I need a summary of enzyme definitions (kinase, phosphorylase, synthetase, etc) and what reactions they're in
85693
The toplevel classification is\nEC 1 Oxidoreductases: catalyze oxidation/reduction reactions \nEC 2 Transferases: transfer a functional group (e.g. a methyl or phosphate group) \nEC 3 Hydrolases: catalyze the hydrolysis of various bonds \nEC 4 Lyases: cleave various bonds by means other than hydrolysis and oxidation \nEC 5 Isomerases: catalyze isomerization changes within a single molecule \nEC 6 Ligases: join two molecules with covalent bonds\n\nthe other parts of the name classify the reaction that they catalyse, kinases and phosphatases are pretty much synonymous
827921
threonine\n\nthere should be a table in your textbook with mRNA codons and corresponding AA's.
1176807
Sounds like somebody is working on a biochem lab. :) \n\nDenaturation lowers enzyme activity because it changes the shape of the protein. Heat disrupts the tertiary structure by breaking covalent, non-covalent and van der waals interations between side chains of the protein. Proteins must be in the right conformation in order to perform their functions correctly. When they are denatured substrates can no longer bind to the active site, key amino acids are no longer in the correct position. \n\npH affects enzyme activity in the following ways: 1-enzyme binding to the active site 2-catalytic activity 3-ionization of the substrate 4-variation of protein structure. This is because pH will change the ionization state of certain side chains. (H+ ions will interact with \n\nOptimum conditions for alpha amylase (ptyalin) from wikipedia.com:\n Optimum pH-5.6 - 6.9\n Room temperatue- 37 degrees Celsius
553744
http://en.wikipedia.org/wiki/Reaction_mechanism\nhttp://en.wikipedia.org/wiki/Bromomethane
933045
CK=Creatine Kinase.\n\nIn most of the cell, the CK enzyme consists of two subunits, which can be either B (brain type) or M (muscle type). \n\nThere are, therefore, three different isoenzymes: CK-MM, CK-BB and CK-MB. The genes for these subunits are located on different chromosomes: B on 14q32 and M on 19q13.\n\nThere are no Latin words involved here!
619603
An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. The word comes from the Greek ένζυμο, énsymo, which comes from én ("at" or "in") and simo ("leaven" or "yeast"). Certain RNAs also have catalytic activity, but to differentiate them from protein enzymes, they are referred to as RNA enzymes or ribozymes.\n\nEnzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products without enzymes. A malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a severe disease. For example, the most common type of phenylketonuria is caused by a single amino acid mutation in the enzyme phenylalanine hydroxylase, which catalyzes the first step in the degradation of phenylalanine. The resulting build-up of phenylalanine and related products can lead to mental retardation if the disease is untreated.\n\nLike all catalysts, enzymes work by providing an alternate pathway of lower activation energy of a reaction, thus allowing the reaction to proceed much faster. Enzymes may speed up reactions by a factor of many millions. An enzyme, like any catalyst, remains unaltered by the completed reaction and can therefore continue to function. Because enzymes do not affect the relative energy between the products and reagents, they do not affect equilibrium of a reaction. However, the advantage of enzymes compared to most other catalysts is their sterio-, regio- and chemoselectivity and specificity.\n\nEnzyme activity can be affected by other molecules. Inhibitors are naturally occurring or synthetic molecules that decrease or abolish enzyme activity; activators are molecules that increase activity. Some irreversible inhibitors bind enzymes very tightly, effectively inactivating them. Many drugs and poisons act by inhibiting enzymes. Aspirin inhibits the COX-1 and COX-2 enzymes that produce the inflammation messenger prostaglandin, thus suppressing pain and inflammation. The poison cyanide inhibits cytochrome c oxidase, which effectively blocks cellular respiration.\n\nWhile all enzymes have a biological role, some enzymes are used commercially for other purposes. Many household cleaners use enzymes to speed up chemical reactions ( e.g., breaking down protein or starch stains in clothes).\n\nMore than 5,000 enzymes are known. Typically the suffix -ase is added to the name of the substrate (e.g., lactase is the enzyme that catalyzes the cleavage of lactose) or the type of reaction (e.g., DNA polymerase catalyzes the formation of DNA polymers). However, this is not always the case, especially when enzymes modify multiple substrates. For this reason Enzyme Commission or EC numbers are used to classify enzymes based on the reactions they catalyze. Even this is not a perfect solution, as enzymes from different species or even very similar enzymes in the same species may have identical EC numbers.
563510
Enzymes are typically large proteins which are structured specifically for the reaction they catalyse. Their size provide sites for action and stability of the overall structure.\n\nTwo identified sites within enzymes are:\n\nThe catalytic site, which is a region within the enzyme involved with catalysis, and the substrate binding site which is the specific area on the enzyme to which reactants called substrates bind to.\n\nThe catalytic site and substrate binding site are often close or overlapping1 and collectively they are called the active site. If the catalytic site is not near the substrate binding site it can move into position once the enzyme is bound to a substrate.\n\nOften enzymes require additional components to become active. These may be:\n\nco-factors - simple cations, or small organic or inorganic molecules that bind loosely to the enzyme,\n\nprosthetic groups – similar to co-factors but more tightly bound to the enzyme, or co-enzymes – which are more complex than co-factors and prosthetic groups, they often act as a second substrate or bind covalently with the enzyme to affect the active site.\n\nThe enzyme must have additional binding sites for the additional components. Enzymes lacking essential additional elements are called apoenzymes, whereas intact active enzymes are called holoenzymes.
444835
hi. you can try a book called "Practical biochemistry, principles and techniques" by Keith Wilson and John Walker
448536
like this: \nhttp://upload.wikimedia.org/wikipedia/en/0/07/Ribosome_subunits.png
474830
Heat, availability of reactants, # of enzymes, other competing enzymes (if any).  These are a few.  Heat is one of the biggest as enzymes have specific temperatures at which they operate best.  At different temperatures they tend to slow or shut down completely.  Hope this helps.
892793
Metabolism is the sum of all chemical reactions within the body.  the basics can be broken down into 2 groups.. Catabolism and anabolism.  Catabolism is the chemical processes that break down complex molecules to release energy.  Anabolism is the process to build up complex chemical compounds from simpler chemical compounds using stored energy.  \nIf your want to know more you should run a search on Krebs cycle, Glycolosis, lipid metabolism, and Protien Anabolism/Catabolism
940990
http://www.chem.purdue.edu/courses/chm333/enzyme_kinetics.swf\nnow be a good boy, study the link, and then explain it to  me....  :)
926847
Substrate-level phosphorylation is the direct transfer of a phosphate group from some compound onto ADP to make ATP.  \n\nIn the glycolytic pathway, there are two specific steps where substrate-level phosphorylation occurs.  If you're counting ATPs produced from a single glucose molecule, then 4 ATPs are produced by the substrate level phosphorylation reactions during glycolysis. \n\nIn the citric acid cycle, there is another point where substrate-level phosphorylation occurs.  Again, if you're counting ATPs from a single glucose molecule, this accounts for 2 more ATPs.\n\nSo, adding those up, you have 6 ATPs produced from the metabolism of one glucose molecule by substrate-level phosphorylation reactions...
919953
a phosphate group\na ribose sugar\nand a nitrogenous base
1100165
Mg is neseccary for the catalytic reaction. A lot of enzymes have an ion in their catalyitic center which usually co-ordinate the reacting groups.
675098
An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. The word comes from the Greek ένζυμο, énsymo, which comes from én ("at" or "in") and simo ("leaven" or "yeast"). Certain RNAs also have catalytic activity, but to differentiate them from protein enzymes, they are referred to as RNA enzymes or ribozymes.\n\nEnzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products without enzymes. A malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a severe disease. For example, the most common type of phenylketonuria is caused by a single amino acid mutation in the enzyme phenylalanine hydroxylase, which catalyzes the first step in the degradation of phenylalanine. The resulting build-up of phenylalanine and related products can lead to mental retardation if the disease is untreated.\n\nLike all catalysts, enzymes work by providing an alternate pathway of lower activation energy of a reaction, thus allowing the reaction to proceed much faster. Enzymes may speed up reactions by a factor of many millions. An enzyme, like any catalyst, remains unaltered by the completed reaction and can therefore continue to function. Because enzymes do not affect the relative energy between the products and reagents, they do not affect equilibrium of a reaction. However, the advantage of enzymes compared to most other catalysts is their sterio-, regio- and chemoselectivity and specificity.\n\nEnzyme activity can be affected by other molecules. Inhibitors are naturally occurring or synthetic molecules that decrease or abolish enzyme activity; activators are molecules that increase activity. Some irreversible inhibitors bind enzymes very tightly, effectively inactivating them. Many drugs and poisons act by inhibiting enzymes. Aspirin inhibits the COX-1 and COX-2 enzymes that produce the inflammation messenger prostaglandin, thus suppressing pain and inflammation. The poison cyanide inhibits cytochrome c oxidase, which effectively blocks cellular respiration.\nEnzymes are usually specific as to the reactions they catalyze and the substrates that are involved in these reactions. Shape, charge complementarity, and hydrophillic/hydrophobic character of enzyme and substrate are responsible for this specificity
950352
Enzymes are catalysts that speed up chemical reactions \n\nLipase- is an enzyme that is used by the body to break down dietary fats into an absorbable form\nPepsin- enzyme is produced in the mucosal lining of the stomach that acts to degrade protein\nAmylase- is a digestive enzyme classified as a saccharidase -an enzyme that cleaves polysaccharides.\nThe sugar maltose is made from two glucose molecules bonded together. The enzyme maltase is shaped in such a way that it can break the bond and free the two glucose pieces. The only thing maltase can do is break maltose molecules, but it can do that very rapidly and efficiently.