CHEM237 Chapter Notes - Chapter 11: Enzyme, Covalent Bond, Atp Hydrolysis
7 Dec 2016
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Document Summary
Active site: asymmetric pocket of the enzyme where the catalyzed reaction occurs. Binding site: amino acids which come into contact w/ the substrate, provide binding energy and speci city. Catalytic site: the residues responsible for the catalysis. Oxidoreductase: catalyze redox reactions - the transfer of h+ or oh- (ie. ketone to alcohol) Transferase: catalyze the transfer of a functional group (ie. phosphate transfer) Hydrolase: catalyze hydrolysis reactions (breakage of bonds by adding water) Lyase: adding/removing groups to break or form double bonds. Isomerase: isomerization (changing the chirality of a stereo centre) Substrate speci city: nearly all enzymes participate in reaction that are absolutely stereospeci c. Enzyme substrate binding shows some induced t and some lock and key theory, non covalent forces are involved in binding (van der waals, electrostatics, Can be a metal ion of coenzyme, provide additional functionality to enzymes that can not be accommodated by amino acids alone.
