title: Electrostatic effects in the alpha-chymotrypsin-catalyzed acyl transfer. II. Efficiency of nucleophiles bearing charged groups in various locations.
abstract: We investigated the alpha-chymotrypsin-catalyzed acyl transfer to a series of glycine oligomers. It could be established that the electrostatic interactions between the carboxylate group of the nucleophiles and the S'-subsites of the enzyme fall off with the length of the nucleophile molecule. Additional negatively charged residues in the nucleophile lead to a considerable reduction of the acyl transfer efficiency. An arginine residue in P'1- or P'3-position, but not in P'2-position, makes favourable interactions with the appropriate S'-subsites of the enzyme.
authors.affiliation: Department of Biochemistry, Leipzig University, F.R.G.
authors.forename: V
authors.initials: V
authors.lastname: Schellenberger
authors.forename: H D
authors.initials: HD
authors.lastname: Jakubke
authors.forename: V
authors.initials: V
authors.lastname: Kasche
mesh_terms: D000215:Acylation; D001665:Binding Sites; D002384:Catalysis; D002918:Chymotrypsin / Q000737:chemistry / Q000378:metabolism*; D004563:Electrochemistry; D004579:Electron Transport; D005998:Glycine / Q000031:analogs & derivatives* / Q000378:metabolism; D008956:Models, Chemical
chemical_list: D002918:Chymotrypsin; D005998:Glycine