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Bacterial enzymes that can deglycate glucose
Bacterial enzymes that can deglycate glucose

... are true deglycating enzymes, but it is yet unknown whether they are active against modified proteins. If so, an obvious useful function would be to deglycate modified lysine-rich histones to make these available for acetylation and the control of gene expression. However, the cell appears to have p ...
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... Amino acids are linked by _________________________________________ • A chain of amino acids is a protein. • Each protein has a unique _______________________!!!!!!! ...
Ch 6 Enzymes and Metabolism - Liberty Union High School District
Ch 6 Enzymes and Metabolism - Liberty Union High School District

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... molecular weight of 96,000. The composition was determined on the botir of three individually purified sampler. The abence of orginine in this enzyme may be an important point in future work with this enzyme, especially with respect to peptide mapping. This work supported in part by the NIH Training ...
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... A. A plot of velocity as a function of substrate concentration has a _____________ shape in saturation kinetics unless it is under allosteric regulation. B. Enzyme efficiency has the parameter _________________, which is a second order rate constant at low concentration of substrate. C. Phosphoenolp ...
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... 1. Be able to apply knowledge of chemistry and biology to solve biochemical problems. 2. .Students will be able to distinguish among carbohydrates, lipids, proteins, and nucleic acids with respect to chemical structure 3. Be able to: demonstrate an understanding of the properties of biomolecules and ...
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Plant Enzyme Structure. Explaining Substrate

... binding site on the enzyme. Thus, the binding site usually consists of a cleft, tunnel, funnel, or other depression on the enzyme’s surface. Only those substrates that have complementary shapes will fit into the binding site. Perhaps most intriguing from an evolutionary viewpoint is the precise alig ...
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Enzyme



Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.
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