Introduction to Enzymes | (S)-limonene 7-monooxygenase of Enzymes

(S)-limonene 7-monooxygenase of enzymes

In enzymology, a (S)-limonene 7-monooxygenase (EC is an enzyme that catalyzes the chemical reaction

(-)-(S)-limonene NADPH H O2 displaystyle rightleftharpoons (-)-perillyl alcohol NADP H2OThe 4 substrates of this enzyme are (-)-(S)-limonene, NADPH, H, and O2, whereas its 3 products are (-)-perillyl alcohol, NADP, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). Other names in common use include (-)-limonene 7-monooxygenase, (-)-limonene hydroxylase, (-)-limonene monooxygenase, and (-)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation. It employs one cofactor, heme.


Preparation of enzymes

Through a cut in the throat, the gills and part of the gullet are removed from the herring, eliminating any bitter taste. The liver and pancreas are left in the fish during the salt-curing process because they release enzymes essential for flavor. The herrings are then placed in the brine for approximately 5 days, traditionally in oak casks. They require no further preparation after fillet and skin removal and can be eaten as a snack with finely sliced raw onion and pickles.

As skin removal requires experience, fillets or double fillets should be attempted first. The soused herrings are silvery outside and pink inside when fresh, and should not be bought if they appear grey and oily.

Whereas salt herrings have a salt content of 20% and must be soaked in water before consumption, soused herrings do not need soaking.


Nudix hydrolase of enzymes

Nudix hydrolases are a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to x (any moiety), hence their name. The reaction yields nucleoside monophosphate (NMP) plus X-P. Substrates hydrolysed by nudix enzymes comprise a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity. Enzymes of the Nudix superfamily are found in all types of organisms, including eukaryotes, bacteria and archaea.

There are two components to the Nudix family: the so-called Nudix fold of a beta sheet with alpha helices on each side and the Nudix motif which contains catalytic and metal-binding amino acids. The Nudix motif is GXXXXXEXXXXXXXREUXEEXGU where U is isoleucine, leucine or valine, and X is any amino acid. This forms a short helix which (usually) contains the catalytic amino acids. Nudix hydrolases include Dcp2 of the decapping complex, ADP-ribose diphosphatase, MutT, ADPRase, Ap4A hydrolases, RppH, and many others.


Benzoate 4-monooxygenase of enzymes

In enzymology, a benzoate 4-monooxygenase (EC is an enzyme that catalyzes the chemical reaction

benzoate NADPH H O2 displaystyle rightleftharpoons 4-hydroxybenzoate NADP H2OThe 4 substrates of this enzyme are benzoate, NADPH, H, and O2, whereas its 3 products are 4-hydroxybenzoate, NADP, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is benzoate,NADPH:oxygen oxidoreductase (4-hydroxylating). Other names in common use include benzoic acid 4-hydroxylase, benzoate 4-hydroxylase, benzoic 4-hydroxylase, benzoate-p-hydroxylase, and p-hydroxybenzoate hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and benzoate degradation via coa ligation. It has 3 cofactors: iron, Tetrahydrobiopterin, and Tetrahydropteridine.


ADAMTS of enzymes

ADAMTS (short for a disintegrin and metalloproteinase with thrombospondin motifs) is a family of multidomain extracellular protease enzymes. 19 members of this family have been identified in humans, the first of which, ADAMTS1, was described in 1997. Known functions of the ADAMTS proteases include processing of procollagens and von Willebrand factor as well as cleavage of aggrecan, versican, brevican and neurocan, making them key remodeling enzymes of the extracellular matrix. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. Homologous subfamily of ADAMTSL (ADAMTS-like) proteins, which lack enzymatic activity, has also been described. Most cases of thrombotic thrombocytopenic purpura arise from autoantibody-mediated inhibition of ADAMTS13.

Like ADAMs, the name of the ADAMTS family refers to its disintegrin and metalloproteinase activity, and in the case of ADAMTS, the presence of a thrombospondin motif.


Research of enzymes

Nagaraja has done research on DNA topoisomerases, topology modulation, regulation of gene expression to understand the underlying molecular mechanisms and their importance in cellular function. Understanding the biology of the pathogen that causes TB has been a major research effort. As a result, several seminal contributions have been made leading to potential applications. His interaction with industry includes development of commercial biotech products such as restriction enzymes and other DNA transaction enzymes, design and development of high fidelity restriction enzyme, new inhibitors for the generation of lead molecules as a step for novel therapeutics against tuberculosis. These have been successfully applied and resulted in international patents. Under his guidance, 21 students have completed doctoral degree and 10 students are at various stages of their PhD. In addition, a large number of project assistants, summer fellows and postdoctoral researchers are trained under him


Identity of hepoxilin-epoxide hydrolase of enzymes

Recent studies have shown that Soluble epoxide hydrolase (i.e. epoxide hydrolase 2 or EH2) readily metabolizes a) hepoxilin A3 (8-hydroxy-11S,12Sepoxy-(5Z,8Z,14Z)-eicosatrienoic acid) to trioxilin A3 (8,11,12-trihydroxy-(5Z,9E,14Z)-eicosatrienoic acid) and b) hepoxilin B3 (10-hydroxy-11S,12Sepoxy-(5Z,9E,14Z)-eicosatrienoic acid) to trioxlin B3 (10,11,12-trihydroxy-(5Z,9E,14Z)-eicosatrienoic acid. Soluble epoxide hydrolase (i.e. epoxide hydrolase 2 or EH2) sEH also appears to be the hepoxilin hydrolase that is responsible for inactivating the epoxyalcohol metabolites of arachidonic acid, hepoxilin A3 and hepoxiin B3. Soluble epoxide hydrolase is widely expressed in a diversity of human and other mammal tissues and therefore appears to be the hepoxilin hydrolase responsible for inactivating hepoxilin A3 and B3 (see soluble epoxide hydrolase#Function and epoxide hydrolase#Hepoxilin-epoxide hydrolase). The ability of EH1, EH3, EH4, and leukotriene A4 hydrolase to metabolize hepoxilins to trioxilins has not yet been reported


ATP10 protein of enzymes

In molecular biology, ATP10 protein (mitochondrial ATPase complex subunit ATP10) is an ATP synthase assembly factor. It is essential for the assembly of the mitochondrial F1-F0 complex. A yeast nuclear gene (ATP10) encodes a product that is essential for the assembly of a functional mitochondrial ATPase complex. Mutations in ATP10 induce a loss of rutamycin sensitivity in the mitochondrial ATPase, but do not affect the respiratory enzymes. ATP10 has a molecular weight of 30,293 Da and its primary structure is not related to any known subunit of the yeast or mammalian mitochondrial ATPase complexes. ATP10 is associated with the mitochondrial membrane. It is suggested that the ATP10 product is not a subunit of the ATPase complex but rather a protein required for the assembly of the F0 sector of the complex.


Indications of enzymes

As with all prescription veterinary medicine, advice on the use of pradofloxacin should always be sought from a suitably qualified veterinarian.

DogsIn Europe Pradofloxacin is indicated for the treatment of:

wound infections and superficial and deep pyoderma caused by susceptible strains of the Staphylococcus intermedius group (including S. pseudintermedius),

acute urinary tract infections caused by susceptible strains of Escherichia coli and the Staphylococcus intermedius group (including S. pseudintermedius) and

as adjunctive treatment to mechanical or surgical periodontal therapy in the treatment of severe infections of the gingiva and periodontal tissues caused by susceptible strains of anaerobic organisms, for example Porphyromonas spp. and Prevotella spp.CatsPradofloxacin is indicated for the treatment of:

acute infections of the upper respiratory tract caused by susceptible strains of Pasteurella multocida, Escherichia coli and the Staphylococcus intermedius group (including S. pseudintermedius).

wound infections and abscesses caused by susceptible strains of Pasteurella multocida and the Staphylococcus intermedius group (including S. pseudintermedius) for oral suspension only.


Glycoside hydrolase family 18 of enzymes

In molecular biology, Glycoside hydrolase family 18 is a family of glycoside hydrolases.

Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.

Some members of this family, CAZY GH_18, belong to the chitinase class II group which includes chitinase, chitodextrinase and the killer toxin of Kluyveromyces lactis. The chitinases hydrolyse chitin oligosaccharides. Another chitinase II member is the novel gene Chitinase domain-containing protein 1. The family also includes various glycoproteins from mammals; cartilage glycoprotein and the oviduct-specific glycoproteins are two examples.


UDP-sulfoquinovose synthase of enzymes

UDP-sulfoquinovose synthase (EC is an enzyme that catalyzes the chemical reaction

UDP-glucose sulfite displaystyle rightleftharpoons UDP-6-sulfoquinovose H2OThus, the two substrates of this enzyme are UDP-glucose and sulfite, whereas its two products are UDP-6-sulfoquinovose and H2O.

In a subsequent reaction catalyzed by sulfoquinovosyl diacylglycerol synthase, the sulfoquinovose portion of UDP-sulfoquinovose is combined with diacyglycerol to produce the sulfolipid sulfoquinovosyl diacylglycerol (SQDG).

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-sulfur bonds. The systematic name of this enzyme class is UDP-6-sulfo-6-deoxyglucose sulfohydrolase. Other names in common use include sulfite:UDP-glucose sulfotransferase, and UDP-sulfoquinovose synthase. This enzyme participates in nucleotide sugars metabolism and glycerolipid metabolism.

The 3-dimensional structure of the enzyme is known from Protein Data Bank entries 1qrr (Mulichak et al., 1999), 1i24, 1i2b and 1i2c.


Diagnosis of enzymes

TypesHyperprolinemia type IIt is difficult to determine the prevalence of hyperprolinemia type I, as many people with the condition are asymptomatic.

People with hyperprolinemia type I have proline levels in their blood between 3 and 10 times the normal level. Some individuals with type I exhibit seizures, intellectual disability, or other neurological problems.

Hyperprolinemia type IIHyperprolinemia type II results in proline levels in the blood between 10 and 15 times higher than normal, and high levels of a related compound called pyrroline-5-carboxylate. This rare form of the disorder may appear benign at times, but often involves seizures, convulsions, and intellectual disability.

Hyperprolinemia can also occur with other conditions, such as malnutrition or liver disease. In particular, individuals with conditions that cause elevated levels of lactic acid in the blood, such as lactic acidemia, are likely to have elevated proline levels, because lactic acid inhibits the breakdown of proline.


Isoflavone 2'-hydroxylase of enzymes

In enzymology, an isoflavone 2'-hydroxylase (EC is an enzyme that catalyzes the chemical reaction

an isoflavone NADPH H O2 displaystyle rightleftharpoons a 2'-hydroxyisoflavone NADP H2OThe 4 substrates of this enzyme are isoflavone, NADPH, H, and O2, whereas its 3 products are 2'-hydroxyisoflavone, NADP, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is isoflavone,NADPH:oxygen oxidoreductase (2'-hydroxylating). Other names in common use include isoflavone 2'-monooxygenase, CYP81E1, and CYP Ge-3. This enzyme participates in isoflavonoid biosynthesis.

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What Are Some Good, Fat-burning Foods?
Various antioxidant rich teas - green, oolong, white, rooibos are some of the best. Whole wheat or whole grain spelt pasta - much higher fiber than normal pastas Oat bran and steel cut oats - higher fiber than those little packs of instant oats. Cans of coconut milk - to be transferred to a container in the fridge after opening. Brown rice and other higher fiber rice - NEVER white rice Tomato sauces - delicious, and as I am sure you've heard a million times, they are a great source of lycopene. Just watch out for the brands that are loaded with nasty high fructose corn syrup. Stevia - a natural non-caloric sweetener, which is an excellent alternative to the nasty chemical-laden artificial sweeteners like aspartame, saccharine, and sucralose. Raw honey - better than processed honey... higher quantities of beneficial nutrients and enzymes. Honey has even been proven in studies to improve glucose metabolism (how you process carbs). I use a teaspoon or so every morning in my teas. Yes, it is pure sugar, but at least it has some nutritional benefits... and let's be real, a teaspoon of healthier raw honey is only 5 grams of carbs... certainly nothing to worry about.1. What enzymes are involved during the process of digestion in the mouth, small intestines and stomach of cats?Do not know how true this is of Cats but for people you have the following: Mouth - Salivary amylase, also know as Ptyalin, breaks down starches and other sugar based macromolecules Stomach - Proteases such as pepsin and rennin that break down protein Small intestine - Pancreatic Amylase (starch again), Trypsin (protein again), Erepsin (peptides to amino acids) and Lipase (allows fats to be broken down along with Bile salts) There are a whole load of other enzymes but that covers the basics. I would imagine that cats are pretty similar, but check if this is for school.2. WHY are many digestive enzymes collectively called hydrolytic enzymes?I say true...the enzyme is for the "digestion" of protein, lipids and carbohydrates3. what does it mean when ur liver enzymes are extremely high?Hep C usually, you need to take milk thistle daily and also have blood work every 3 months. You are not too drink Alcohol and do drugs. Go too the Doctor and have it tested for heps. also you may need a biopsy.4. I'm a vegetarian, and I recently just found out about animal enzymes in cheese...?Some frozen entrees & some of the cheeses at the health food store have labels that say they use vegetarian enzymes only. Also, Trader Joe's has a few of their cheeses that say they do not use animal rennet in them. These are their mozzarella & their muenster, & they are labeled as low fat as well. I am very fond of them, too. I think Annie's products & Amy's products are just fine. I only rarely eat Annie's white shells & cheese, so I do not think about it much. I am fairly sure that Amy's are fine. In the frozen food by Amy's, many are available with soy instead of cheese, so that's a possibility, too. I do love 3 kinds of Amy's frozen Pocket Sandwiches & am fairly sure that I checked out the labels when I first started buying them. I also think that many of Amy's are labeled organic & GMO-free, in case that is important to you as well.5. What is the function of enzymes in cells?enzymes are biological catalysts, they speed up biological reactions.their power as catalyst enables biological reactions to occur in milliseconds without which, the same reaction may take days/months even years to complete6. How do you "cure" an elevated ALT(high liver enzymes)?Banish salt through your foods wherever you can. Not simply does it raise your blood pressure and play havoc your blood, but sodium causes you to retain water contributing to overall ill health and weight gain7. Are enzymes with superior catalytic properties more sensitive to temperature changes?There is no obvious direct connection between catalytic properties and stability of an enzyme.You are trying to make a connection, but let's consider your statement:Then the Arrhenius equation can be used to describe how the rate constant of an enzymatic reaction changes with temperature.According to the Arrhenius equation, all reactions (catalyzed by an enzyme or not) become faster as temperature increases. The higher the activation energy, the more pronounced the increase. However, if the enzyme unfolds, it will no longer catalyze the reaction.But how can I use this information to decide whether the more catalytic enzyme is more or less temperature dependent?The biggest temperature dependence occurs at the temperature where the enzyme unfolds. There is the idea that enzymes have to be flexible to be effective catalysts, so there might be a correlation between optimal temperature for the activity and the unfolding temperature. The best way to figure this out would be to compare enzymes from mesophiles and thermophiles in terms of optimal temperature for catalysis vs melting temperature
Urgent Easy Question (just Wondering If Im Right)?
The phospholipid bilayer does act like a filter. There are also proteins embedded in the bilayer that act as gateways through the membrane. This is known as active transport and passive transport. If the substance going through the membrane does not have to cross against a gradient, then it is passive transport and various proteins and enzymes will determine the permeability in this case. If there is a gradient it must cross, then the cell membrane must have certain proteins that account for active transport. For example, if sodium is trying to get into the cell and it has to cross against a concentration gradient, there must be certain sodium allowing proteins that make the cell membrane permeable to sodium. ATP is used in this case to work the generator like protein to push the sodium into the cell. When I say concentration gradient I mean that there is more sodium in the cell than out, so for a sodium molecule to go INTO the cell, energy must be expended to allow the molecule across (active transport). This is because the sodium is going against the laws of diffusion. There are other characteristics such as cell-cell communication which allow certain molecules to pass through a cell undeterred and prevent others. Hope this helps1. How does physical digestion (chewing) aid chemical digestion (enzymes breaking down polymers to monomers)?by chewing food is breaking up to smaller bits so the surface of the food increases and enzymes have more places to work with2. On the ingredients when they say enzymes do they really mean rennet?Any dairy product that says it s Kosher is, by definition, vegetarian. I m not an expert, but I do know that it is NOT Kosher to eat meat and ANY dairy product together, so cheese that is Kosher has no meat product in it, whether it is regular rennet or rennet synthesized from other animals. Microbial rennet/enzymes is not animal rennet. Anything that says that it is vegetarian, is probably vegetarian. Anything that says in the ingredients just "enzymes" and nothing else COULD be vegetarian, but it also COULD NOT. I don t trust it unless it says elsewhere on the packaging that is is vegetarian, or Kosher, or "contains no animal rennet", or something like that. There are several Kosher symbols. Look them up, but usually there s a little D in a circle or a KD or a K in a little slice of bread. Cabot cheese is vegetarian. Polly-O cheese is vegetarian. The Wegmans brand of mozzerella cheese sticks is Vegetarian. And weirdly enough, the Wal-Mart brand of block mozzerella is also vegetarian. Cheez-Its are vegetarian. Annie s mac and cheese is vegetarian. I think Philadelphia cream cheese is vegetarian, but you may have to check that one. The same with whipped cream. And if all else fails you can just get heavy whipping cream and whip it yourself. Any fresh produce is probably fine, so maybe switch from canned to fresh blueberries, but the canned ones are probably fine. Anything that is made of plants is probably vegetarian. If you see ingredients that you don t understand, just look them up. Chocolate and soda are probably okay, but if you re not sure, check the label, and if you re still not sure, then it s your call. If you find out later that you chose wrong, then just stop eating it. It s up to you what it okay or not okay for you to eat. It s your diet, nobody else s.3. why do we need enzymes?Obama has not determined that we do. Please stop defying him4. Which of these enzymes catalyzes the semiconservative replication of the bacterial chromosome during cell division?DNA polymerase III is the primary enzyme involved in DNA replication in E. coli. Others involved in various methods of DNA repair5. Are enzymes acidic or basic?Thanks for A2A Deval GawandeFirst of all Enzymes are catalyst and we know that most enzymes are proteins containing amino acids as their basic constituents tho one may say that they are slightly acidic .Tho several of them have side chain groups that can act as "acids or bases". These acidic or basic amino acid side chains are called "general acids" or "general bases " in the context of the enzyme . For example lets take an example of amino acids , the structure has a carbon having a NH2- Group as well as a -COOH group and we know that --NH2 makes many compounds basic .So they can show both behavior.Tho their working actually depends on the pH of where the enzyme is present.A lot of them work in acidic environment for example Pepsin which works at an optimum pH of 2 which is highly acidic. Tho there are some more enzymes that tends to either show their function at an optimum pH of 7 (neutral) or some basic level near 7 but greater than 7 .For example carbonic anhydrase that works in the neutral pH .Tho the general activity of all enzymes differ . Like trypsin works in the small intestine, parts of which have a pH of around 7.5. Trypsin's optimum pH is about 8.Hope this helps:):PAre enzymes acidic or basic?
What Is the Role of Enzymes in a Human?
Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions. In these reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts these into different molecules, the products. Almost all processes in the cell need enzymes in order to occur at significant rates. Since enzymes are extremely selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell. Like all catalysts, enzymes work by lowering the activation energy for a reaction and thus dramatically accelerating the rate of the reaction. By binding the transition-state conformation of the substrate/product molecules, the enzyme distorts the bound substrate(s) into their transition state form, thereby reducing the amount of energy required to complete the transition. Most natural enzymes accelerate their reaction many millions of times faster compared to the uncatalyzed reaction. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. However, enzymes do differ from most other catalysts by being much more specific. Enzymes are known to catalyze about 4,000 biochemical reactions.1. Need AP Bio help: enzymes?I am in AP Bio myself and just talk about how much you can relating to structure and function. For example, primary structure, secondary, tertiary and quaternary structure. You can talk about bonds (covalent, Van der Waals, etc) and the atoms and links between them. Polarity, electronegativity can be discussed to. Basically configuration is their structure and shape2. which one is the right answer for bio question?How many different types of enzymes are needed in your body? thousands3. what is the name of enzyme that is present in rice?The rice plant will contain hundreds of enzymes, but unless you know what the enzyme is responsible for doing, then there is no way of figuring out which enzyme you want to know about4. A creationist claimed: 1. In order to create DNA, enzymes are needed. 2. Enzymes are proteins. 3. In order to create proteins (and then enzymes) DNA is needed. Could you comment on this irresolvable problem of endless cycle?In looking over the various "answers", I am struck at the number of assumptions regarding that complex mechanisms just sort of happened. Let's discuss an analogy that, I hope, illuminates the my thoughts: Consider a car - say, a Ford Mustang. it's a complex piece of machinery, right? It's beautiful to behold and is very good at transporting its driver across large distances. It's purpose-built. Further, nobody questions that the Mustang must have had a designer - of course it did! In addition to the designer(s), it was also built by someone. Now, if someone laid all the necessary parts and materials in a heap, all those parts would never become a Mustang. They could never assemble themselves into a Mustang. There MUST be an intelligent designer involved and somehow all those parts must be assembled together to become that beautiful Mustang. Again, nobody in their right mind would question this. So, how much more complex is a living cell?5. How are enzymes effected by the reaction?Enzymes are catalysts, so they are not effected by the reaction by definition. Catalysts must be the same before and after the reaction, otherwise they can't catalyze another of the same reaction. Now this is true if you only consider the before and after states of the reaction. During the reaction, enzymes can change in many ways. Based on the induced fit theory, when the substrate enters the active site of the enzyme, it causes the enzyme to change shape and fit the substrate better. When the reaction proceeds to the transition state (most unstable and highest point of Gibb's free energy), enzymes do many things to stabilize the transition state. Some enzymes transfer electrons to the transition state temporarily to stabilize unfavorable charges. Some form transient covalent bonds with the transitions state. Regardless of how they change while stabilizing the transition state, once the products are formed and the products leave the enzyme, the enzyme returns to its original state (how it was before the reaction). How are enzymes effected by the reaction?
Which of the Following Best Describes the Purpose of the Detergent?
Detergents soften the fats. They can also denature enzymes, which are proteins, but they do this by disrupting the shape of the proteins. I know there are fats in the cell membrane but I am not sure if there are fats in the NUCLEAR MEMBRANE1. describe how enzymes increase the speed of chemical reactions?Michaelis-Menten equation describes it very well :) It is because of the activation energy is decreased2. What role do enzymes have in a biological system?They are symbiotic life forms. They are actual living creatures. They perform services for us by breaking apart our food and other things. Symbiotic means that bipedals (humans) or animals (other mammals) are dependant on them for life and they depend on us. When these die, they must be replaced with actually living replacements. Sickness and death occur when they are lost. You can buy digestive enzymes and others to replace yours. They must be stored in cool place away from light as it kills them. Standard temperature ice box bottom (not freezer) is fine. Just the next step warmer version of those life forms that could be stored in ice on that moon. They are very much life forms and living. Not just dead chemicals to cause a reaction, but chaste and workers in the home just like wives and just like the Almighty God who made the house. Debbie3. Meiosis, Mitosis and Enzymes in sexual reproduction questions?Meiosis allows for variation in the gametes, so at fertilisation, the offspring will be even more varied. Mitosis allows the offspring to replicate it's cell where they become specialised, and therefore can develop as an organism.4. What does it mean when a person has elevated liver enzymes on a standard blood test?liver enzymes are only indicators of liver damage - it does not mean cirrhosis - however your drinking habits would lead one to believe you probably have alcoholic hepatitis - alcohol consumption is never safe - its toxic to even healthy livers - if you have liver damage - drinking can eventually shut down the liver - id request a biopsy to determine the amount of damage you have5. The doctor is saying my spleen and liver are 3 times the normal size and fatty and my enzymes are high?Low-fat protein is a great basis for a weight reduction plan. Foods like lean turkey, lentils and eggs within the right quantities will keep ones sugar levels even, make you feel fuller for longer, lower the GI of the carbs you combine it using and help repair damaged cells6. I need help! I need two attributes of enzymes in catalyzing chemical reactions and in metabolic pathways.?enzymes play no role in any reaction but they fasten the reaction... Enzymes have a specific pH. They are actually proteins which remains active b/w 20 and 40 degree celsiuis . Above 40 and below 20, it gets denatured!! theres one enzyme in the saliva called SALIVARY AMYLASE and one in stomach called PEPSINOGEN Hope it helps7. What is the best treat for rats that most rats like also that are healthy and safe?If your interested in very healthy treats I would recommend a variety of fruits. Just make sure that whatever fruit you use wont be toxic to the rat at all. Here are some other good treats... - Yogurt drops, choc chips (chocolate is not poisonous to rats) and yogurt covered raisins. - Frozen peas and corn - popcorn, sunflower seeds & pumpkin seeds Or you can try this recipe. It sounds like it will not only be tasty for your rat but also healthy, it may take a little work but it will be worth it. - Yogurt drops, choc chips (chocolate is not poisonous to rats) and yogurt covered raisins. - Frozen peas and corn - popcorn, sunflower seeds & pumpkin seeds Just make sure NO MATTER WHAT you do not give your rat any of these foods- Blue Cheese - the mold in it is toxic to rats Green Bananas - inhibits starch-digesting enzymes Green Potato Skin and Eyes - contain solanine, a toxin Licorice - suspected to cause neurological poisoning in a rat Orange Juice - forbidden for male rats only, the d-limonene in the skin oil can cause cancer. Mango - also forbidden for male rats only, due to the d-limonene in the flesh. Raw Artichokes - inhibits protein digestion Raw Bulk Tofu or Meat- can contain bacteria, packaged raw tofu is safe Raw Dry Beans or Peanuts - contains anti nutrients that destroy vitamin A and enzymes needed to digest protein and starches and causes red blood cells to clump Raw Red Cabbage and Brussels Sprouts - contains antinutrient that destroys thiamin (cooked is fine) Raw Sweet Potato - contains compounds that form cyanide in the stomach (cooked is fine and a hit with most rats) Avocado skin and Pitt - toxic to rats. The flesh is fine Rhubarb - contains high levels of oxalates Sticky foods such as Peanut Butter, some Candy, and Dried Fruits - poses a choking hazard. Peanut butter can be "cut" with jam or honey to make it more liquid, and reduce the possibility of choking. Seaweed - the seaweed the comes on sushi or in soup poses a choking hazard. Wild Insects - can carry internal parasites and diseases
Introduction to Enzymes - Protocatechuate 4,5-dioxygenase of Enzymes
Protocatechuate 4,5-dioxygenase of enzymesIn enzymology, a protocatechuate 4,5-dioxygenase (EC is an enzyme that catalyzes the chemical reactionprotocatechuate O2 displaystyle rightleftharpoons 4-carboxy-2-hydroxymuconate semialdehydeThus, the two substrates of this enzyme are protocatechuate and O2, whereas its product is 4-carboxy-2-hydroxymuconate semialdehyde.This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is protocatechuate:oxygen 4,5-oxidoreductase (decyclizing). Other names in common use include protocatechuate 4,5-oxygenase, protocatechuic 4,5-dioxygenase, and protocatechuic 4,5-oxygenase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, iron.------Methylenetetrahydrofolate dehydrogenase (NADP) of enzymesIn enzymology, a methylenetetrahydrofolate dehydrogenase (NADP) (EC is an enzyme that catalyzes the chemical reaction5,10-methylenetetrahydrofolate NADP displaystyle rightleftharpoons 5,10-methenyltetrahydrofolate NADPH HThus, the two substrates of this enzyme are 5,10-methylenetetrahydrofolate and NADP, whereas its 3 products are 5,10-methenyltetrahydrofolate, NADPH, and H.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD or NADP as acceptor. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate:NADP oxidoreductase. Other names in common use include N5,N10-methylenetetrahydrofolate dehydrogenase, 5,10-methylenetetrahydrofolate:NADP oxidoreductase, 5,10-methylenetetrahydrofolate dehydrogenase, methylenetetrahydrofolate dehydrogenase, and methylenetetrahydrofolate dehydrogenase (NADP). This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.------Pyruvate dehydrogenase (cytochrome) of enzymesIn enzymology, a pyruvate dehydrogenase (cytochrome) (EC is an enzyme that catalyzes the chemical reactionpyruvate ferricytochrome b1 H2O displaystyle rightleftharpoons acetate CO2 ferrocytochrome b1The 3 substrates of this enzyme are pyruvate, ferricytochrome b1, and H2O, whereas its 3 products are acetate, CO2, and ferrocytochrome b1.This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is pyruvate:ferricytochrome-b1 oxidoreductase. Other names in common use include pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, and pyruvate oxidase (ambiguous). This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.------Mannose-6-phosphate 6-reductase of enzymesIn enzymology, a mannose-6-phosphate 6-reductase (EC is an enzyme that catalyzes the chemical reactionD-mannitol 1-phosphate NADP displaystyle rightleftharpoons D-mannose 6-phosphate NADPH HThus, the two substrates of this enzyme are D-mannitol 1-phosphate and NADP, whereas its 3 products are D-mannose 6-phosphate, NADPH, and H.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is D-mannitol-1-phosphate:NADP 6-oxidoreductase. Other names in common use include NADPH-dependent mannose 6-phosphate reductase, mannose-6-phosphate reductase, 6-phosphomannose reductase, NADP-dependent mannose-6-P:mannitol-1-P oxidoreductase, NADPH-dependent M6P reductase, and NADPH-mannose-6-P reductase.------Glycerol-3-phosphate oxidase of enzymesIn enzymology, a glycerol-3-phosphate oxidase (EC is an enzyme that catalyzes the chemical reactionsn-glycerol 3-phosphate O2 displaystyle rightleftharpoons glycerone phosphate H2O2Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:oxygen 2-oxidoreductase. Other names in common use include glycerol phosphate oxidase, glycerol-1-phosphate oxidase, glycerol phosphate oxidase, L-alpha-glycerophosphate oxidase, alpha-glycerophosphate oxidase, and L-alpha-glycerol-3-phosphate oxidase. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD.------ALG6 (enzyme class) of enzymesDolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase (EC, ALG6, Dol-P-Glc:Man9GlcNAc2-PP-Dol alpha-1,3-glucosyltransferase) is an enzyme with systematic name dolichyl beta-D-glucosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-glucosyltransferase.This enzyme catalyses the following chemical reactionwhich is:dolichyl beta-D-glucosyl phosphate D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->6)-D-Man-alpha-(1->6)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol displaystyle rightleftharpoons D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->6)-D-Man-alpha-(1->6)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol dolichyl phosphate------Isoflavone 3'-hydroxylase of enzymesIn enzymology, an isoflavone 3'-hydroxylase (EC is an enzyme that catalyzes the chemical reactionformononetin NADPH H O2 displaystyle rightleftharpoons calycosin NADP H2OThe 4 substrates of this enzyme are formononetin, NADPH, H, and O2, whereas its 3 products are calycosin, NADP, and H2O.This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is formononetin,NADPH:oxygen oxidoreductase (3'-hydroxylating). This enzyme is also called isoflavone 3'-monooxygenase. This enzyme participates in isoflavonoid biosynthesis. It employs one cofactor, heme.------Names of enzymesIt is marketed under many brand names worldwide, including:Xiva, An Li Nuo Er, An Sai Ma, Ansimar, Asima, Bestofyline, Chuan Ning, D-Fyal, Dilatair, Doxiba, Doxobid, Doxobron, Doxofilina, Doxofillina, Doxofyllin, Doxoll, Doxophylline, Doxovent, Doxyjohn, Fei Te Ai Si, Jian Fang Neng, Lang Ming, Lv Meng, Mai Ping Xi, Maxivent, Mucosma, Na De Lai, Phylex, Phyllin, Puroxan, Rexipin, Shu Zhi, Shuai An, Shuweixin, Suo Di, Suo Ji, Suo Li An, Xi Si Nuo, Xin Qian Ping, Xin Xi Ping, Yi Suo, and Yili.It is also marketed as a combination drug with terbutaline as Doxoll-TL, Mucosma-T and Phylex-TR.It is also marketed as a combination drug with montelukast as Doxoll-ML, Doxomont, Doxoril-M, Doxovent-M, Lunair-M, and Venidox-M.------UDP-N-acetylglucosaminedolichyl-phosphate N-acetylglucosaminephosphotransferase of enzymesIn enzymology, an UDP-N-acetylglucosaminedolichyl-phosphate N-acetylglucosaminephosphotransferase (EC is an enzyme that catalyzes the chemical reactionUDP-N-acetyl-D-glucosamine dolichyl phosphate displaystyle rightleftharpoons UMP N-acetyl-D-glucosaminyl-diphosphodolicholThus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and dolichyl phosphate, whereas its two products are UMP and N-acetyl-D-glucosaminyl-diphosphodolichol.This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups transferases for other substituted phosphate groups. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase. Other names in common use include UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase, UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase, UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase, uridine diphosphoacetylglucosamine-dolichyl phosphate acetylglucosamine-1-phosphotransferase, chitobiosylpyrophosphoryldolichol synthase, dolichol phosphate N-acetylglucosamine-1-phosphotransferase, UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase, and UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase. This enzyme participates in the biosynthesis of N-glycan and glycan structures.------Coenzyme F420 hydrogenase of enzymesIn enzymology, a coenzyme F420 hydrogenase (EC is an enzyme that catalyzes the chemical reactionH2 coenzyme F420 displaystyle rightleftharpoons reduced coenzyme F420Thus, the two substrates of this enzyme are H2 and coenzyme F420, whereas its product is reduced coenzyme F420.This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with other, known, acceptors. The systematic name of this enzyme class is hydrogen:coenzyme F420 oxidoreductase. Other names in common use include 8-hydroxy-5-deazaflavin-reducing hydrogenase, F420-reducing hydrogenase, and coenzyme F420-dependent hydrogenase. This enzyme participates in folate biosynthesis and is a critical part of energy conservation in some methanogens such as Methanosarcina barkeri. It has 3 cofactors: iron, nickel, and deazaflavin.-------alpha,7-alpha-dihydroxy-5-beta-cholestanateCoA ligase of enzymesIn enzymology, a 3alpha,7alpha-dihydroxy-5beta-cholestanate-CoA ligase (EC is an enzyme that catalyzes the chemical reactionATP (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate CoA displaystyle rightleftharpoons AMP diphosphate (25R)-3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoAThe 3 substrates of this enzyme are ATP, (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate, and CoA, whereas its 3 products are AMP, diphosphate, and (25R)-3alpha,7alpha-dihydroxy-5beta-cholestanoyl-CoA.This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is (25R)-3alpha,7alpha-dihydroxy-5beta-cholestan-26-oate:CoA ligase (AMP-forming). Other names in common use include 3alpha,7alpha-dihydroxy-5beta-cholestanoyl coenzyme A synthetase, DHCA-CoA ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming). This enzyme participates in bile acid biosynthesis.------Methylmalonyl-CoA carboxytransferase of enzymesIn enzymology, a methylmalonyl-CoA carboxytransferase (EC is an enzyme that catalyzes the chemical reaction(S)-methylmalonyl-CoA pyruvate displaystyle rightleftharpoons propanoyl-CoA oxaloacetateThus, the two substrates of this enzyme are (S)-methylmalonyl-CoA and pyruvate, whereas its two products are propanoyl-CoA and oxaloacetate.This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the carboxy- and carbamoyltransferases. The systematic name of this enzyme class is (S)-methylmalonyl-CoA:pyruvate carboxytransferase. Other names in common use include transcarboxylase, methylmalonyl coenzyme A carboxyltransferase, methylmalonyl-CoA transcarboxylase, oxalacetic transcarboxylase, methylmalonyl-CoA carboxyltransferase, methylmalonyl-CoA carboxyltransferase, (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase, (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxytransferase, and carboxytransferase incorrect. This enzyme participates in propanoate metabolism. It has 3 cofactors: zinc, Biotin, and Cobalt.------S9 fraction of enzymesThe S9 fraction is the product of an organ tissue homogenate used in biological assays. The S9 fraction is most frequently used in assays that measure the metabolism of drugs and other xenobiotics. It is defined by the U.S. National Library of Medicine's "IUPAC Glossary of Terms Used in Toxicology" as the "Supernatant fraction obtained from an organ (usually liver) homogenate by centrifuging at 9000 g for 20 minutes in a suitable medium; this fraction contains cytosol and microsomes." The microsomes component of the S9 fraction contain cytochrome P450 isoforms (phase I metabolism) and other enzyme activities. The cytosolic portion contains the major part of the activities of transferases (phase II metabolism). The S9 fraction is easier to prepare than purified microsomes..------Amiflamine of enzymesAmiflamine (FLA-336) is a reversible inhibitor of monoamine oxidase A (MAO-A), thereby being a RIMA, and, to a lesser extent, semicarbazide-sensitive amine oxidase (SSAO), as well as a serotonin releasing agent (SRA). It is a derivative of the phenethylamine and amphetamine chemical classes. The ()-enantiomer is the active stereoisomer.Amiflamine shows preference for inhibiting MAO-A in serotonergic relative to noradrenergic and dopaminergic neurons. In other words, at low doses, it can be used to selectively inhibit MAO-A enzymes in serotonin cells, whereas at higher doses it loses its selectivity. This property is attributed to amiflamine's higher affinity for the serotonin transporter over the norepinephrine and dopamine transporters, as transporter-mediated carriage is required for amiflamine to enter monoaminergic neurons.------Pathophysiology of enzymesFumarase deficiency is caused by a mutation in the fumarate hydratase (FH) gene in humans, which encodes the enzyme that converts fumarate to malate in the mitochondria. Other mutant alleles of the FH gene, located on human Chromosome 1 at position 1q42.1, cause multiple cutaneous and uterine leiomyomata, hereditary leiomyomatosis and renal cell cancer. Fumarase deficiency is one of the few known deficiencies of the Krebs cycle or tricarboxylic acid cycle, the main enzymatic pathway of cellular aerobic respiration.The condition is an autosomal recessive disorder, and it is therefore usually necessary for an affected individual to receive the mutant allele from both parents. A number of children diagnosed with the disorder have been born to parents who were first cousins. It can also be associated with uniparental isodisomy.------Flavone synthase of enzymesIn enzymology, a flavone synthase (EC is an enzyme that catalyzes the chemical reactiona flavanone 2-oxoglutarate O2 displaystyle rightleftharpoons a flavone succinate CO2 H2OThe 3 substrates of this enzyme are flavanone, 2-oxoglutarate, and O2, whereas its 4 products are flavone, succinate, CO2, and H2O.This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is flavanone,2-oxoglutarate:oxygen oxidoreductase (dehydrating). This enzyme participates in flavonoid biosynthesis and isoflavonoid biosynthesis.------Neddylation process of enzymesNEDD8 links itself to a protein through an isopeptide linkage between its carboxy-terminal glycine and the lysine of the substrate.The neddylation of the substrate causes in a structural change, and there are three main biochemical effects that result. First, neddylation can cause a conformational change in the substrate which may restrict molecular movement and the positioning of different binding partners. Second, it can cause the target protein to become incompatible with other proteins that it usually binds with. For example, CAND1 does not bind to neddylated proteins. In addition, neddylation can recruit NEDD8-interacting proteins. When NEDD8 binds to the ubiquitin E2 Ubc4, the interaction stimulates cullin-based ubiquitin ligases, although the exact mechanism is unclear.
Knowledge Related to Glucose 1-dehydrogenase (NAD
In enzymology, a glucose 1-dehydrogenase (NAD) (EC is an enzyme that catalyzes the chemical reactionD-glucose NAD displaystyle rightleftharpoons D-glucono-1,5-lactone NADH HThus, the two substrates of this enzyme are D-glucose and NAD, whereas its 3 products are D-glucono-1,5-lactone, NADH, and H.This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is D-glucose:NAD 1-oxidoreductase. Other names in common use include D-glucose:NAD oxidoreductase, D-aldohexose dehydrogenase, and glucose 1-dehydrogenase (NAD).• Other Related Knowledge of enzymesEnzymes from T. aquaticus of dna polymerase iT. aquaticus has become famous as a source of thermostable enzymes, particularly the Taq DNA polymerase, as described below.AldolaseStudies of this extreme thermophilic bacterium that could be grown in cell culture was initially centered on attempts to understand how protein enzymes (which normally inactive at high temperature) can function at high temperature in thermophiles. In 1970, Freeze and Brock published an article describing a thermostable aldolase enzyme from T. aquaticus.RNA polymeraseThe first polymerase enzyme isolated from T. aquaticus in 1974 was a DNA-dependent RNA polymerase, used in the process of transcription.Taq I restriction enzymeMost molecular biologists probably became aware of T. aquaticus in the late 1970s or early 1980s because of the isolation of useful restriction endonucleases from this organism. Use of the term Taq to refer to Thermus aquaticus arose at this time from the convention of giving restriction enzymes short names, such as Sal and Hin, derived from the genus and species of the source organisms.DNA polymerase ("Taq pol")DNA polymerase was first isolated from T. aquaticus in 1976. The first advantage found for this thermostable (temperature optimum 72C, does not denature even in 95 C) DNA polymerase was that it could be isolated in a purer form (free of other enzyme contaminants) than could the DNA polymerase from other sources. Later, Kary Mullis and other investigators at Cetus Corporation discovered this enzyme could be used in the polymerase chain reaction (PCR) process for amplifying short segments of DNA, eliminating the need to add E. coli polymerase enzymes after every cycle of thermal denaturation of the DNA. The enzyme was also cloned, sequenced, modified (to produce the shorter 'Stoffel fragment'), and produced in large quantities for commercial sale. In 1989 Science magazine named Taq polymerase as its first "Molecule of the Year". In 1993, Dr. Kary Mullis was awarded the Nobel Prize for his work with PCR.Other enzymesThe high optimum temperature for T. aquaticus allows researchers to study reactions under conditions for which other enzymes lose activity. Other enzymes isolated from this organism include DNA ligase, alkaline phosphatase, NADH oxidase, isocitrate dehydrogenase, amylomaltase, and fructose 1,6-disphosphate-dependent L-lactate dehydrogenase.------Discovery of enzymesNAPE-PLD is an enzyme activity - a phospholipase, acting on phospholipids found in the cell membrane. It is not homology but the chemical outcome of its activity that classes it as phospholipase D. The enzymatic activity was discovered and characterized in a series of experiments culminating in the 2004 publication of a biochemical purification scheme from which peptide sequencing could be accomplished. Researchers homogenized (finely ground) hearts from 150 rats and subjected the resulting crude lysate to sucrose sedimentation at 105,000 x g to separate out the cell membranes from the remainder of the cell. The integral membrane proteins were then solubilized using octyl glucoside and subjected to four column chromatography steps (HiTrap SP HP cation-exchange column, HiTrap Q anion-exchange column, HiTrap Blue affinity column, Bio-Gel HTP hydroxyapatite column). Each of these separates the different types of membrane proteins into different sample containers when the proteins are eluted from the column over time, and by measuring the activity of samples in each container it was possible to track which ones received the active enzyme. Measurement of the enzyme activity was done by thin layer chromatography of a radioactive substrate sensitive to the NAPE-PLD enzymatic activity: Cleavage of the substrate affected where it appeared on the plate when the radiation was detected on a bioimaging analyzer.The result of this extensive procedure was still not a pure protein, but it produced a limited number of bands by SDS-PAGE, and one band of 46 kilodaltons was found to correlate in intensity with the enzymatic activity. This band was cut out from the gel and digested with trypsin, and peptides from it were separated from one another by reverse phase high performance liquid chromatography. The resulting fragments were then microsequenced by an automated Edman degradation. Three corresponded to vimentin, an intermediate filament protein of 56 kDa believed to be a contaminant, and the other two matched the cDNA clone subsequently identified as NAPE-PLD.Once this clue had been obtained, the identification could be confirmed by a less onerous procedure: Overexpression of the putative NAPE-PLD cDNA in COS-7 cells yielded a strong NAPE-PLD enzymatic activity, whose characteristics were shown to be similar to those of the original heart extract.------Notable publications of enzymesBooksEnzymatic Reaction Mechanisms (1978). Published by Freeman Inc (.mw-parser-output .citation qquotes:"""""""'""'".mw-parser-output .id-lock-free a,.mw-parser-output .citation .cs1-lock-free abackground-image:url("");background-image:linear-gradient(transparent,transparent),url("");background-repeat:no-repeat;background-size:9px;background-position:right .1em .id-lock-limited a,.mw-parser-output .id-lock-registration a,.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration abackground-image:url("");background-image:linear-gradient(transparent,transparent),url("");background-repeat:no-repeat;background-size:9px;background-position:right .1em .id-lock-subscription a,.mw-parser-output .citation .cs1-lock-subscription abackground-image:url("");background-image:linear-gradient(transparent,transparent),url("");background-repeat:no-repeat;background-size:9px;background-position:right .1em .cs1-subscription,.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration spanborder-bottom:1px dotted; .cs1-ws-icon abackground-image:url("");background-image:linear-gradient(transparent,transparent),url("");background-repeat:no-repeat;background-size:12px;background-position:right .1em code.cs1-codecolor:inherit;background:inherit;border:inherit; .cs1-hidden-errordisplay:none; .cs1-maintdisplay:none;color:#33aa33; .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-right,.mw-parser-output .citation .mw-selflinkfont-weight:inheritISBN978-0716700708).Antibiotics: Actions, Origins, Resistance (2003), by Christopher Walsh. Published by ASM Press (ISBN978-1555812546).Post-translation Modification of Proteins: Expanding Nature's Inventory (2006), by C.T. Walsh. Published by Roberts and Company (ISBN0974707732).------Biography of enzymesAlexander Dounce was born on December 7, 1909, in New York. He began his undergraduate studies at Hamilton College but later moved to Cornell University, where he also did his doctoral studies in the lab of James B. Sumner, a pioneer in protein crystallization. Dounce received his PhD in organic chemistry in 1935, the title of his thesis being "Study of dihydrofurans and the dehydration rearrangement of 2,3-ethylenic 1,4-diols". According to Marshall W. Nirenberg, another biochemist who knew Dounce personally, "during his Dounce's final doctoral exam when his doctoral committee got together to ask him questions after he had finished his thesis research, his mentor, Sumner, asked him the question, 'How do proteins synthesize other proteins?' He Dounce said that question remained in his mind ever since then."After his graduation, Dounce stayed in Sumners lab and did work on enzymes, particularly on enzyme isolation and purification. Together with Sumner, he achieved the first crystallization of the enzyme catalase in 1937. In 1941, Dounce moved to the Department of Biochemistry at University of Rochester Medical School, where he worked on the mechanism of uranium poisoning for the Manhattan Project. After the end of World War II, he focussed on studying cell nuclei and particularly the isolation of intact nuclei from tissue, which was a new field of research at the time. In 1952, Alexander Dounce and Ernest Kay, who was Dounce's first PhD student, published a new method for DNA isolation and purification from nuclei employing sodium dodecyl sulfate that became widely used.Also in 1952, Dounce wrote a review article in which he, as one of the first scientists to do so, proposed that DNA might serve as a template for the synthesis of RNA, which in turn serves as a template for the synthesis of proteins. This order of synthesis, which has later been termed the "central dogma of molecular biology" by Francis Crick, is textbook knowledge today. However, it was not until 1958, when Crick coined the term central dogma and described the concept in more detail, that it gained widespread acceptance.In the same review article, Dounce was also one of the first scientists to propose a genetic code in which nucleotide triplets code for each of the 20 proteinogenic amino acids. He correctly assumed that genes consist of nucleic acid sequences which determine the amino acid sequences of proteins, and that a protein's sequence determines its function. Based on these assumptions, Dounce speculated that, during protein synthesis, each amino acid would pair with an individual nucleotide; the two other nucleotides surrounding it would determine the specificity of the binding. While the actual mechanism turned out to be different, Dounce's hypothesis that nucleotide triplets code for amino acids was correct, and his speculations "helped lead to the deciphering of the code." In the words of Nirenberg, "In the review he was far ahead of everybody else .... He predicted that the code would be a triplet code, and that, as I recall, RNA was the template for protein synthesis. But he buried this article in the proceedings of an Oak Ridge symposium that nobody read. ... By and large, the ideas were good, although he was wrong on minutiae. I was amazed when I finally read it."When James D. Watson and George Gamow founded the RNA Tie Club in 1954, Dounce became one of its members; his designation was GLN (glutamine).Dounce's work on the isolation of cellular organelles, particularly nuclei and mitochondria, led to the development of the Dounce homogenizers in 1954. A Dounce homogenizer or "Douncer" is a glass mortar and pestle with a very small clearance between the mortar and the pestle in Dounce's original design as little as 0.0005 inches or about 13 micrometers. This allows for tissue and cells to be lysed by shear stress while leaving the smaller organelles intact. Dounce homogenizers are still commonly used today to isolate cellular organelles.When Dounce's former mentor, James B. Sumner, died in 1955, Dounce wrote Sumner's obituary in Nature.For the remainder of his career, Dounce continued his research on nuclei and their contents, catalase, and protein crystallization.Dounce died on April 24, 1997, in Rochester, New York. He was survived by his wife, Anna Elizabeth Dounce, who was the daughter of botanist Donald Reddick, and by their three children Helen, Eric, and George.
Enzymes Used to Cut DNA Molecules in Recombinant DNA Research Are?
1>C (I know a fermented fish sauce) 2>B 3>D 4>? most likely C though 5>A 6>B 7>C 8>C1. What is the role in digestion and enzymes produced in the...?Salivary smylase begins to digest starch in the mouth - and continues to do so on its trip down the esophagus, until it is inactivated by the acidity of the stomach. Pepsin is produced by cells in the stomach lining, and begins the digestion of proteins in the stomach. Pepsin requires the low pH created by HCl secreted by other stomach lining cells. Several enzymes function in the small intestine, most of them coming from the pancreas: trypsin, chymotrypsin, and carboxypeptidase finish the digestion of proteins, forming amino acids and dipeptides; pancreatic amylase finishes the digestion of starch, forming the disaccharide maltose; lipase digests fats, forming fatty acids and glycerol; and nucleases that digest DNA and RNA. Cells in the small intestine lining produce sucrase (which breaks down sucrose to glucose and fructose) and dipeptiase (which breaks down dipeptides to individual amino acids). The liver does not produce any enzymes that digest our food, but it produces bile, which is stored in the gall bladder and secreted into the small intestine. Bile is a detergent that disperses the fat in our food, enabling the lipase enzymes to get at all the fat molecules. The products of digestion are absorbed into the bloodstream from the small intestine. Whatever is left, not digested and/or not absorbed, including the bile, continues on into the large intestine (colon), and is eventually eliminated from the body as feces. No digestion occurs in the large intestine.2. What are 5 enzymes in the human body and what are their functions?(1) Lactic dehydrogenase-converting pyruvate to lactic acid-after a severe excercise, it accumaltes in muscles. (2) Acetyl choline estearase-converts acetyl choline to acetate and choline-In epilepsy it is poured in large amounts resulting in seizures (3)Invertase converts Sugar (Sucrose) to glucose and fructose. (4)Pepsin breaks proteins at specific sites. (5) Amylase converts Amylose(Starch) to glucose3. What is the test called where they test your urine for protiens and enzymes?Urine dipstick tests can be done to detect specific gravity, pH, glucose, protein, blood, bilirubin, ketones, urobilinogen, nitrite, and leukocytes. Are you thinking of electrolytes? These are substances in your blood (sodium, calcium, potassium, chlorine, magnesium, and bicarbonate) that keep your body "balanced" and your heart beating!4. What makes proteins the ideal types of compounds to act as enzymes?Proteins are very highly structurally complex, which means within their structure are highly specific 'pockets' which act as active sites for reaction catalysis. These sites can be acidic, basic, hydrophilic, hydrophobic, all depending on the nature of the amino acids inside the pocket. The shape of the pocket depends on the secondary structure (hydrogen bonds) and tertiary structure (folding) of the protein. These sites only allow very specifically shaped and charged molecules in, and so are very highly specific to their substrate. This is necessary for catalysis in the body, where there are a lot of similar molecules and the reaction needs to be very specific to one of these molecules.5. how do enzymes recognize their substrates specifically?They have an active site which only a certain substrate can be fit in. It can be explained using the lock and key theory or induced fit theory google up on them. Some substrates need a co enzyme so that the subtrate can fit into the active site of the enzyme and be catalysed.6. Why do so many biochemical reactions require enzymes?We speak of reactions that There is only one one way to get that: the self regulating production of self regulating catalysts. Enzymes.7. what are the role of lock and key enzymes? my teacher said that there are two of themmlock & key n something?Enzymes serve as catalysts which lower the activation energies of chemical reactions in order to speed them up. Lock and key enzymes are special because a key can only open one type of lock. In the same way, one type of enzyme can only react with one type of substrate in order to catalyze a reaction.8. How does enzymes and ATP working together get two molecules to interact?mang ap bio ended for me like two month ago and let just hope im rite. Im think ATP provide energy for enzyme to catalyze substrate. anyway b4 enzyme start to get going there need to be activation energy then ATP give off energy for enzyme to catalyze so the free engery in this reaction would start as positive to negative unless the reaction is spontaneous. ehh im thinking im wrong but c'mon its summer who would remember all those thing on midterm and final???
How Can You Clean Cat Pee Out of a Purse?
As you can see from my avatar, I like cats. Unfortunately I have had a purse peed on before and have found that it is best to just put the purse in the washing machine after first rinsing it in a sink of water to get most of the pee out.The purse is destined for ruination anyhow, and I have had good luck with fake or real leather by washing it in the machine. So, submerge first in the sink and use some dish liquid or Tide or Fabulosa or anything, then put it in the washer by itself with regular detergent and some of that oxy clean stuff..any brand because that will help. If it still smells, ,put it through two or three more times and use vinegar if you like, but the main idea is to get the urine out of the purse. What is hard to clean pree out of is stuff you can not submerge and rinse over and over like a carpet or chair.There are formulas with peroxide, soap and baking soda too, but the oxyclean is the same idea nullify the urine. Do not make the water super hot..just warm or cold. When the purse seems clean, put it on the line or somewhere outside to dry naturally, not the dryer. If it still stinks, the smell will get in the dryer besides ruining the purse. The water wo not destroy it, but it will never be like new. Google remove cat urine and you will see lots of home made formulas with peroxide and products with enzymes, but those wo not really work.1. how are nutrients absorbed from fruits and vegetables?chewing mechanically breaks food down to create more surface area. there are enzymes in your saliva that begin the break down of carbohydrates as you chew. after you swallow, the food ends up in your stomach where mechanical and chemical digestion take place. the stomach squeezes the food and releases hydrochloric acid as well as pepsin and other enzymes to break the food down even more. now it is pushed in the small intestine where your liver (gallbladder actually) releases bile to breakdown fats and your pancreas releases many enzymes to break down everything elses you can imagine. it also releases bicarb which is like an antacid (like tums) to prevent the hydrochloric acid from your stomach from digesting your intestines. now everything has been broken down mechanically and chemically and the blood vessels that surround your small intestines engorge with blood. nutrients are passed through thin membranes from your intestines to your capillaries and into your blood stream. they connect and make a first pass to your liver to clean out the bad chemicals before being pumped by your heart to all the living cells in your body.2. What effect do end products have on enzymes?End products can either not have an effect on enzymes, as with many biochemical pathways, but can also inhibit enzymes, especially in anabolic pathways (where larger molecules are synthesised from smaller building blocks) to regulate them. Since a certain amount/concentration of the end-product is needed, if the reaction continues past the desired extent, it could lead to wastage of resources and energy, and a build-up of products could have toxic effects too.An example of end-product inhibition can be seen in the synthesis of adenosine triphosphate (ATP) during glycolysis. Phosphofructokinase (PFK) is an enzyme involved in the first step of glycolysis - the phosphorylation of glucose, and is inhibited by ATP. Consequently, high ATP concentrations results in a lower rate of glycolysis, and thus ATP production.On the other hand, an example of end-product repression can be seen in the trp operon, which is found in E. coli. The expression of the operon, which contains structural genes which code for enzymes responsible for the synthesis of tryptophan, is regulated by a repressor protein, which is normally inactive. However, tryptophan, the end-product of the downstream pathway, can bind to the allosteric site of the protein, activating it. The activated repressor protein is then able to bind to the operator of the operon, preventing the genes from being expressed. Image sources: What effect do end products have on enzymes?3. I am a vegetarian; however how can doritos be considered "vegetarian" if they have porcine enzymes in them?because they do not contain the flesh of those meats-- Are you a vegetarian or a vegan??
What Role Do the Enzymes Secreted by the Pancreas Play in the Digestive Process/tract?
It has many enzymes: - Trypsin, which is a protease, that breaks down peptides (a smaller form of protein) to amino acids. - Amylase, which digests carbohydrates and turns them to a simpler form, but not completely to a reducing sugar. - Lipase, which, with help of bile salts, digests fats into fatty acids and glycerol - It also releases Sodium Hydrogen carbonate (not an enzyme, but an alkali) that partly neutralizes the acidity of the food that passed by the stomach which has an acid, HCL) Okay, that's what is in my syllabus :) Mainly, it helps digest food :)1. True or False Biology? Please help hw!?1) TRUE - By standard definition, organic compounds contain carbon. 2) TRUE - By lowering activation energy, enzymes decrease the energy needed to push a reaction forward. 3) FALSE - Biosynthesis is the formation of a chemical compound by a living ORGANISM. There's really no such thing as a "living compound." 4) TRUE - This is a bit tricky, because inorganic compounds can contain carbon. An example would be a heme, which is inorganic because it has an iron center but is also surrounded by a carbon-containing porphyrin ring. However, not ALL organic compounds contain carbon, so make sure there are no details in the question that you may have omitted here. 5) TRUE - For sure!2. to what group of biomolecules do enzymes belong?Biomolecules And Enzymes3. why enzymes are useful as industrial catalysts?amylases-production of sugars from starch, which includes in making extreme-fructose corn syrup.[d09bf41544a3365a46c977ebb5e35c3d09bf41544a3365a46c977ebb5e35c In baking, catalyze breakdown of starch contained in the flour to sugar. Yeast fermentation of sugar produces the carbon dioxide that will advance the dough. Proteases-Biscuit manufacturers use them to diminish the protein element of flour. Enzymes from barley are released in the course of the mashing level of beer production-hi degrade starch and proteins to produce ordinary sugar, amino acids and peptides that are used by technique of yeast for fermentation. Amylase, glucanases, proteases-chop up polysaccharides and proteins contained in the malt. Betaglucanases and arabinoxylanases-advance the wort and beer filtration features. Amyloglucosidase and pullulanases-Low-calorie beer and adjustment of fermentability. Proteases-get rid of cloudiness produced throughout the time of storage of beers. Acetolactatedecarboxylase (ALDC)-will advance fermentation performance by technique of reducing diacetyl formation.[4. Best way to get dog piddle odor and stains out of carpet?There is a pet carpet wash called Natures Miracle. It has enzymes that neutralize pet pee odors. It also works well for other stains. Plus, to help your dog not pee at night you can place him in a small Kennel. It will keep him from peeing, dogs will not go where they sleep. you can buy it at any pet supply store5. Can someone define the type of chemical reaction involved in the formantion of a linkage between 2 animo acids?It is a typical condensation reaction between a carboxylic acid and an amine to make an amide with loss of water R-COOH H-NH- R ---------- RCO-NH-R H2O In this case one amino acid furnishes the COOH and the other furnishes the NH2 a peptide bond is infact an amide linkage and enzymes that cleave the peptide bond ( peptidases ) belong to the hydrolytic enzyme class of amidases.6. What are the two enzymes involved in protein & fat digestion?Bile is not an enzyme. It is created by the liver and released by the gallbladder and its main job is to neutralise the acid the stomach produces before everything goes into the small intestine. The enzymes produced in the stomach work best at a pH of 2, which is why the stomach produces acid for them to work. However the enzymes in the small intestine dont work well in acid, which is why bile is needed to neutralise the acid before everything goes into the small intestine, to ensure the enzymes work well there. Lipase is a fat digesting enzyme, it breaks down fats (lipids) into fatty acids and glycerol; it's produced by the pancreas Protease is a protein digesting enzyme, it breaks down proteins into amino acids; it's produced by the pancreas and small intestine Pepsin is a type of protease, produced in the stomach Amylase is a startch digesting enzyme, it breaks down startch into sugars; produced by the salivery glands in the mouth - (if you pop a piece of bread in your mouth, and keep it there without chewing or swallowing, it will begin to taste sweeter, because the amylase turns the startch in the bread into sugar). Its also produced by the pancreas Hope this helped :)
Do You Have a Second to Answer a Few Questions I Have About Enzymes?
You have the unfavorable environment question correct. They slow down or stop working depending how far you get from the norm and what extreme. Concentration definitely affects rate of reaction. But not the way you are thinking. Many enzymes are very efficient and catalyze reactions quickly. A classic example from a biochem class would be like the enzyme carbonic anyhydrase. Check out the wikipedia page but it's something like 10,000 reactions per second. That's fast! But that rate can go up or down depending on how much substrate is there or how little is there. Enzymes lower activation energy. Bubbles?? Hmmm... not sure the exact context they are talking about here. Could be like bubbles from an electrophoresis rig or even an enzyme (similar to the one I mentioned) that converts something that's a solute into a something that's a gas. You would get bubbles then.1. what are digestive enzymes? what do they do? how do they work?in the course of our digestive system many enzymes r secreted by the gland which break down many components of the food. our saliva is the very first enzyme which breaks down the starch in the food.alike diff enz. breakes fat ,carbohydrates etc2. A creationist claimed: 1. In order to create DNA, enzymes are needed. 2. Enzymes are proteins. 3. In order to create proteins (and then enzymes) DNA is needed. Could you comment on this irresolvable problem of endless cycle?Enzymes are just catalysts. The reactions they affect would have happened anyway - very inefficiently and very slowly, but they would have happened. One of the fun things about RNAs is that they can be both catalyst and code and genetic switch, RNAs can fold up to form passable enzymes and bind to each other to promote and/or inhibit replication. See RNA world.DNA is more stable as a molecule which is why it took over as the primary genetic store in most organisms and proteins more flexible and generally more stable than RNA as an enzyme. In one of the other answers the analogy of a scaffold is used - RNA is that scaffold, and there are plenty of remnants of those ancient mechanisms left in modern cells in the form of mRNAs, tRNAs and ribosomes3. A creationist claimed: 1. In order to create DNA, enzymes are needed. 2. Enzymes are proteins. 3. In order to create proteins (and then enzymes) DNA is needed. Could you comment on this irresolvable problem of endless cycle?See Brian Farley's answer to How would one explain the phrase "all proteins are enzymes but not all enzymes are proteins"?Research ribozymes4. Enzymes in Detergents, Soaps, and Shampoos?Q: What is the difference between an Enzyme and a Hormone? A: You can not hear an Enzyme.5. What are some bread brands that don't contain animal enzymes?the more basic the bread, the less likely it will have anything to do with animal. Bread is basically flour, a fat source(some recipes do not even have that) a liquid, salt and yeast. No animal enzymes at all. Go to a reputable bakery where you can ask about what is in the bread. I have never seen a home made bread recipe call for animal enzymes so that is another option. Take a day and bake enough bread for a couple of weeks. Wrap tightly and freeze what you do not use immediately. Bread freezes very well.6. Which system of enzymes and coenzymes uses the energy from NADH and FADH2 to form ATP?The electron transport chain - Has 4 Complexes = I, II, III and IV on the inner mitochondrial membrane and is the last phase of aerobic respiration7. Can you get an ulcer from taking enzymes?Here's what I found: Enzymes typically have a larger percentage of positive effects than negative side effects. The most common negative effect is an upset stomach on the use of large amounts of proteolytic enzymes, typically anything greater that 100, 000 HUT. This is easily relived through either the discontinuation of the products or beginning an even lower dosage that is tolerable and slowly building up the potency. Under clinical use, some kind of positive results are gained 70-90% of the time. No death of a patient has ever been attributed to the use of supplemental enzymes in any quantity
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