Lect_9_notes - Bio 1A Lecture 9 Enzymes Mechanism Regulation Prof Schlissel Enzyme Mechanisms and Regulation 1 Acid-base catalysis Requires

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Bio 1A Lecture 9 Enzymes: Mechanism & Regulation Prof. Schlissel Feb 11, 2008 Enzyme Mechanisms and Regulation 1. Acid-base catalysis. Requires R-groups with hydrogen donors or acceptors (know these). Example of lysozyme using Glu and Asp residues to help hydrolyze glycosidic bond. 2. Enzymes can be regulated by temperature and pH. Example of proteases. Example of thermophillic proteins. 3. Allosteric regulation: binding of small molecules to enzymes alter their shape and activity. 4. Enzyme inhibitors: competitive—bind to active site; non-competitive—bind elsewhere. 5. Feedback inhibition, usually by end product of a pathway back onto first enzyme step. 6. Zymogens—inactive precursors activated by specific proteolysis 7. Regulation by covalent modification. Often by phosphorylation / dephosphorylation. Ser, Thr, Tyr can be reversibly phosphorylated, changing protein structure and activity.
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This note was uploaded on 04/01/2008 for the course BIO 1A taught by Professor Schlissel during the Spring '08 term at University of California, Berkeley.

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