Inhibitors

Inhibitors - catalytic subunits, described by a modified...

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Competitive inhibitor : bind to the active site of the enzyme, alter Km Non-competitive inhibition: bind to somewhere besides the active site, alter Vmax o Allosteric regulation: regulatory molecule binds to a site separate from the active site, alters the shape of the enzyme to change its activity, enzymes usually have catalytic and regulatory domains (can have multiple domains or subunits for different regulators) Catalytic domain: region of an enzyme which assists in chemical reactions o Covalent modification: adding/removing groups – like phosphate groups by kinases, cleaving bonds – converting proenzymes to enzymes - like in the blood clotting cascade o Association-dissociation of subunits: one protein binds to another, thereby activating the enzymatic activity of one of them o Cooperativity : one substrate aids or impedes the catalysis of another, implies multiple
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Unformatted text preview: catalytic subunits, described by a modified Michaelis-Menten equation • SNARE: membrane proteins which bind to one another and help pull vesicle and cell membranes together, “Vesicular” vSNARE extends from the vesicle membrane, while“Target” tSNARE extends from the cell membrane (in this case) o Synaptobrevin: vSNARE found in synaptic vesicles containing neurotransmitters, cut by tetanus and botulisum toxins • Intestinal epithelium: epithelium that covers the small and large intestine. It is simple columnar and nonciliated, where the botulism toxin crosses into the bloodstream • Light chain: small polypeptide subunit of a protein complex • Zinc endopeptidase: cleaves synaptobrevin (no synaptobrevin, no vesicle fusion, no neurotransmitter release à paralysis)...
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This note was uploaded on 04/23/2011 for the course BIME 2102 taught by Professor Kim during the Spring '11 term at UVA.

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