Unknown

Dataset Information

0

Kinetics of chymotrypsin- and papain-catalysed synthesis of [leucine]enkephalin and [methionine]enkephalin.


ABSTRACT: The proteinase-catalysed synthesis of [Leu]enkephalin and [Met]enkephalin was studied kinetically. N alpha-t-Butoxycarbonyl-amino acids and peptides or their ethyl esters served as acyl donors, and amino acid phenylhydrazides were used as acyl acceptors. Initial-velocity measurements of alpha-chymotrypsin-catalysed peptide synthesis gave rise to kinetic patterns that are compatible with a ping-pong mechanism modified by a hydrolytic branch. Initial-rate and alternative-substrate inhibition patterns for papain-controlled peptide-bond formation are consistent with a sequential ordered mechanism with the acyl donor as the obligatory first substrate. On the basis of the observed kinetic features, reaction mechanisms are proposed for chymotrypsin- and papain-catalysed peptide synthesis that inversely equal those describing the pathways of proteolysis. The respective initial-velocity expressions for bireactant systems are given, along with the numerical values of the corresponding kinetic parameters.

SUBMITTER: Kullmann W 

PROVIDER: S-EPMC1153641 | biostudies-other | 1984 Jun

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1215192 | biostudies-other
2010-03-09 | GSE20626 | GEO
| S-EPMC2982084 | biostudies-literature
2010-05-06 | E-GEOD-20626 | biostudies-arrayexpress
| S-EPMC1270121 | biostudies-other
| S-EPMC10799539 | biostudies-literature
| S-EPMC1206922 | biostudies-other
| S-EPMC1177119 | biostudies-other
| S-EPMC1144749 | biostudies-other
| S-EPMC7876033 | biostudies-literature