chymotrypsin

covalent catalysis

active site contains a nucleophile that is briefly covalently modified

general acid base catalysis

a molecule other than water donates or accepts a proton

metal ion catalysis

metal ions function in a number of ways, including serving as an electrophilic catalyst

catalysis by approximation and orientation

enzyme brings 2 substrates together in an orientation that facilitates catalysis

hydrophobic pocket

specifity, binds a hydrophobic residue on substrate and positions the adjacent peptide bond for cleavage

oxyanion hole

region of active site, stabilizes the tetrahedral reaction intermediate, lowers energy

N termial

on the left, in hydrophobic patch

chymotrypsin structure

creates an environment where histidine can accept a proton from serine in the catalytic mechanism

alters

chymotrpysin ____ pKas by five units in enzyme active site

humps

TS are graphed as

falls

intermediate states are graphed as

first step

acid base catalyst, Asp orients and renders His as proton acceptor

low barrier hydrogen bond

formed during catalysis by chymotrypsin, stabilizes the His

covalent catalyst

during the mechanism, an intermediate forms a covalent link to the enzyme

Phe, Tyr, or Trp

chymotrypsin has a preference for cleaving after _______ as they fit into the substrate’s binding pocket

scissle bond

where the cleavage occurs

deprotonation of Ser by His

allows for nucleophilic attack by Ser on His

diffusion of fragment

After Ser is leaving group and cleaved, there is

leaving group and is cleaved

after cleavage of peptide bond, Ser acts as a ________ from peptide fragment