MBB 222 Lecture Notes - Lecture 14: Oxyanion Hole, Scissile Bond, Catalytic Triad

• School: Simon Fraser University
• Department: Molec Biol & Biochem
• Course: MBB 222
• Professor: Adam Barlev

Document Summary

Have different substrate specificities (i. e. , bind to different side chains within a protein, so they cleave at different amino acid residues) Many are related in amino acid sequence. Serine proteases are specific for the side chain of the amino acid on the n-terminal side of the peptide bond that will be cleaved (i. e. , r1 on the blue segment, p2). They specifically recognize this side chain and cleave the peptide bond after (c-terminal to) this amino acid. Learning outcomes know what the following terms mean: alkoxide ion, tetrahedral intermediate, oxyanion, oxyanion hole, specificity pocket, acyl-enzyme intermediate. Understand the charges for carbon, nitrogen and oxygen in different functional groups and reaction intermediates, based on the number of e- in their orbitals. Understand what electron pushing means in a reaction mechanism know the definitions for electronegative, electropositive, nucleophile, electrophile, and how nucleophiles and electrophiles behave in a chemical reaction. Understand base catalysis and covalent catalysis in the context of the chymotrypsin- catalyzed reaction.