[Peptide synthesis catalyzed by proteases. Elevated nucleophilic activity of naphthylamides of amino acids in acyl transfer reactions catalyzed by alpha-chymotrypsin].
It was found that the reactivity of alpha-amino acid naphthylamides in acyl transfer reactions catalyzed by alpha-chymotrypsin exceeds by more than two orders of magnitude the effective reactivity of other C-protected derivatives of these compounds. A detailed kinetic analysis of the acyl transfer of the tert-butyl oxycarbonyl-L-methionine residue from its p-nitrophenyl ester to L-arginine naphthylamide was carried out. A minimal kinetic scheme of acyl transfer reactions is proposed, including together with the major process, i.e., acyl residue transfer to the nucleophil, the hydrolysis of the acyl enzyme-nucleophil complex and nucleophil binding by the free enzyme. The numeric values of some kinetic constants were determined. A theoretical analysis of the effect of hydrolysis of the acyl enzyme-nucleophil complex on the degree of nucleophil conversion into the peptide at initial acyl group donor and nucleophil concentrations was carried out.
Gololobov
M Iu
MIu
Shviadas
V K
VK
D000215:Acylation; D000596:Amino Acids; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin; D007700:Kinetics; D010455:Peptides / Q000138:chemical synthesis*
D000596:Amino Acids; D010455:Peptides; D002918:Chymotrypsin
Peptidnyĭ sintez, kataliziruemyĭ proteazami. Povyshennaia nukleofil'nost' naftilamidov aminokislot v reaktsiiakh atsil'nogo perenosa, kataliziruemykh alpha-khimotripsinom.