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Article

The catalytic mechanism of DD-peptidases: unexpected importance of tyrosine 280 in the transpeptidation reaction catalysed by the Streptomyces R61 DD-peptidase.

Cellular and molecular life sciences : CMLS - 1 Jul 1998

Wilkin J M, Lamotte-Brasseur J, Frère J M

Abstract excerpt

The study of the interactions between the Tyr280Phe mutant of the Streptomyces R61 DD-peptidase, various substrates and beta-lactam antibiotics shows that Tyr280 is involved not only in the formation of the acylenzyme with the peptide substrate and beta-lactam antibiotics, but also and specifically in the catalysis of the transpeptidation reaction. Surprisingly, this residue does not belong to the conserved...

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Identifiers

PMID: 9711239
DOI: 10.1007/s000180050200
PMCID: PMC11147258

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