生物化学英文课件酶.pptVIP

How does an enzyme lower the activation energy of a reaction? Formation of the enzyme-substrate complex (ES) Catalyze oxidation-reduction reactions. Contains dehydrogenase and oxidase. For example: lactate dehydrogenase, peroxidase. Catalyze transfers of groups between donors and acceptors. For example: glutamate-pyruvate transaminase (GPT), acyltransferase. Catalyze cleavage of bonds by addition of water. For example: pyrophosphatase, peptidase. Catalyze lysis of a substrate, generating a double bond or adding a substrate to a double bond of a second substrate. For example: pyruvate decarboxylase, aldolase. Catalyze racemization of optical or geometric isomers and certain intramolecular oxidation-reduction reactions. For example: alanine racemase, mutase. Join two molecules at the expense of a high energy phosphate bond of ATP. For example: glutamine synthetase, carboxylase. 3.4.1. Allosteric regulation Allosteric regulation: Metabolites binds to region of outside the active site, and change the conformation, and thus the enzyme activity. Allosteric enzyme Allosteric site Allosteric effector Allosteric inhibitor Allosteric activator Allosteric enzyme Allosteric enzymes: are enzymes whose activity at the catalytic site may be modulated by reversible, noncovalent binding of a special modulator to a regulatory or allosteric site. Allosteric site: is the specific site on the surface of an allosteric enzyme molecule to which the modulator or effector molecule is bound. Allosteric effector: is a biomolecule that binds to allosteric site of an allosteric enzyme and modulates its activiry. Allosteric enzyme Allosteric enzymes are often multi-subunit proteins with an active site on each subunit. Allosteric enzymes often have more than one active site which co-operatively bind substrate molecules. Allosteric regulation The binding of substrate at one active site induces a conformational change in the enzyme that alters the affinity