BCH210H1 Chapter 11: R11

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Review: enzyme mechanics: modes of catalysis, nucleophilic substitution, proximity effect, stabilization effect (ts), acid-base catalysis, reactive groups of ionizable amino acids, play a role in enzyme catalysis. Lysozyme: cleave bacterial cell ways; glycosidic hydrolase, the active site has 6 binding pockets (a f, contains residues in c, d, e, f. Lysozyme cleavage occurs on carbon 1 of the murnac residue and binding pocket d: glu-35 and asp carry out catalysis. How does the catalysis mechanism take place: there must be a conformational change on binding pocket d with a murnac residue, when murnac enters pocket binding. Murnac and the oxygen: this will cause residue e to cleave off, taking the proton with it. Reading 12: we are then left with the positively charged murnac residue known as an oxocarbocation, it is very unstable (think of it as a transition state, however, it is stabilized by the negatively charged asp-52.