THE CATALYTIC MECHANISM OF DD-PEPTIDASES - UNEXPECTED IMPORTANCE OF TYROSINE-280 IN THE TRANSPEPTIDATION REACTION CATALYZED BY THE STREPTOMYCES R61 DD-PEPTIDASE

Authors
WILKIN JM LAMOTTEBRASSEUR J FRERE JM
Citation
Jm. Wilkin et al., THE CATALYTIC MECHANISM OF DD-PEPTIDASES - UNEXPECTED IMPORTANCE OF TYROSINE-280 IN THE TRANSPEPTIDATION REACTION CATALYZED BY THE STREPTOMYCES R61 DD-PEPTIDASE, Cellular and molecular life sciences, 54(7), 1998, pp. 726-732
Citations number
17
Categorie Soggetti
Biology,"Cell Biology",Biology
Journal title
Cellular and molecular life sciences → ACNP
ISSN journal
1420682X
Volume
54
Issue
7
Year of publication
1998
Pages
726 - 732
Database
ISI
SICI code
1420-682X(1998)54:7<726:TCMOD->2.0.ZU;2-6
Abstract
The study of the interactions between the Tyr280Phe mutant of the Stre ptomyces R61 DD-peptidase, various substrates and beta-lactam antibiot ics shows that Tyr280 is involved not only in the formation of the acy lenzyme with the peptide substrate and beta-lactam antibiotics, but al so and specifically in the catalysis of the transpeptidation reaction. Surprisingly, this residue does not belong to the conserved structura l and functional elements which characterise the penicillin-recognisin g enzymes.