Lecture 11 - Catalysis & Proteases

Lecture 11 - Catalysis & Proteases -...

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Enzyme Catalysis-Serine  Proteases Concepts to be learned Activation Energy Transition State Example: Proteases Requirements for proteolysis Families of proteases Protein Folds used by  proteases for catalysis
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Catalysis Enzyme: increases rate of chemical  reaction, decreases activation energy How? Binding to the transition state of the  substrate (L. Pauling 1946) Reaction Path:       Residues of Enzyme Substrate Product
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Enzymes accelerate chemical  reactions by decreasing the activation  energy
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Hydrolysis of Peptide Bonds
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Serine Proteases Peptide bond cleavage by forming  tetrahedral transition states: First Stage: Acylation “Acyl-enzyme intermediate” formed Second Stage: Deacylation “Acyl-enzyme intermediate” is hydrolyzed by  water
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Serine Proteases Rx: Peptide Bond Cleavage 4 Requirements Catalytic triad Ser, His, Asp Ser forms a covalent bond with substrate 
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Lecture 11 - Catalysis & Proteases -...

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