Biomolecules Lecture_10_Enzymes

Biomolecules Lecture_10_Enzymes - Biomolecules and...

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Lecture 10 - Enzymes Biomolecules and Metabolism
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Transition State Mechanism In this enzyme-substrate complex state, the substrate exists in a short-lived, unstable chemical state and significantly less activation energy is required to complete the transition to product than if the enzyme were absent.
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Activation Energy 1. Lower the “activation energy” of a chemical rxn by ! the randomness of collisions between molecules 2. Help bring the substrates together in the proper orientation so that the rxn can occur Mechanism Transition state uncatalyzed Transition state catalyzed
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Overview Enzymes - Classification - Regulation - Mechanism - Proteases - Kinetics - Assay
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Proteases 1. Hydrolyze amide bonds in proteins and peptides 2. Classified by dominant amino acid component in the active site 2. There are four basic categories: - Serine (e.g. Chymotrypsin, Trypsin, Elastase) - Metallo (e.g. ACE, ECE, NEP) - Aspartyl - Cysteine Proteases
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Serine Proteases Proteases 1. Serine proteases have a serine hydroxyl group that is involved in the mechanism of amide bond hydrolysis 2. The sequence of reactions involves formation of a
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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 Lecture_10_Enzymes - Biomolecules and...

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