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12 Cards in this Set
- Front
- Back
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Acid - base catalysts
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enzyme side chains transfer H+ to or from the substrate, causing a covalent bond to break
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allosteric regulation
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an effector binds an enzyme at a site different from the active site, which changes its shape
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metabolic Pathways
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the first reaction is a commitment step, feedback inhibition
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covalent catalysts
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a functional group in a side chain bonds covalently with substrate
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inorganic cofactors
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ions permently bound to enzyme
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reversible inhibition
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inhibitor bonds non covalently to the active site and prevents substrate from binding
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transition state intermediates
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activation energy changes the reactants into unstable forms with higher free energy
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enzymes can be activated when
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protein kinase adds phosphate groups and deactivate by protein phosphatase
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non competitive inhibitors
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bind to enzyme at a different site (not the active site)
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competitive inhibitors
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compete with the natural substrate for binding sites
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in catalyzing a reaction , an enzyme may use one or more mechanisms
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orienting substrates. inducing strain, temporarily adding chemical groups
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irreversible inhibition
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inhibitor covalently bonds to side chains in the active site and permanently inactivates the enzyme
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