Biomolecules Lecture_12_Enzymes

Biomolecules - Biomolecules and Metabolism Lecture 12 Enzymes Overview Enzymes Classification Regulation Mechanism Proteases Kinetics/Assay Enzyme

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Lecture 12 - Enzymes Biomolecules and Metabolism
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Overview Enzymes - Classification - Regulation - Mechanism - Proteases - Kinetics/Assay
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Enzyme Inhibition Reversible inhibition Competitive Mixed (Non-competitive) Uncompetitive Irreversible inhibition Inhibition
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Mixed Inhibition Inhibition 1. Inhibitor binds to both free enzyme and ES complex 2. Usually does not bind the active site 3. ESI complex does not react
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Mixed Inhibition Inhibition
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Mixed Inhibition Inhibition 1. Non-competitive inhibition has consequences for kinetics. 2. K m is unchanged, unless a mixed inhibitor is used. 3. V max is lowered by a factor of (1 + [I]/K i ). At high [S], the inhibitor is still bound to the enzyme. 4. K cat is lowered by a factor of (1 + [I]/K i ).
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Enzyme Inhibition Reversible inhibition Competitive Mixed (Non-competitive) Uncompetitive Irreversible inhibition Inhibition
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Uncompetitive Inhibition Inhibition 1. Inhibitor binds to site on the enzyme that becomes available only after substrate binds (i.e. Inhibitor binds to
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This note was uploaded on 01/05/2010 for the course FSH BT taught by Professor Ianmarison during the Spring '09 term at Dublin City University.

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Biomolecules - Biomolecules and Metabolism Lecture 12 Enzymes Overview Enzymes Classification Regulation Mechanism Proteases Kinetics/Assay Enzyme

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