Article (Scientific journals)
Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions.
Grandchamps, Jacqueline; Nguyen-Distèche, Martine; Damblon, Christian et al.
1995In Biochemical Journal, 307 (Pt 2), p. 335-339
Peer Reviewed verified by ORBi
 

Files


Full Text
Ghuysen-1995_Streptomyces.pdf
Publisher postprint (805.05 kB)
Download

The final version of record is available at http://www.biochemj.org/bj/307/0335/bj3070335_browse.htm


All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Amino Acid Sequence; Bacterial Proteins; Binding Sites; Carrier Proteins/metabolism; Esters/metabolism; Hexosyltransferases; Molecular Sequence Data; Muramoylpentapeptide Carboxypeptidase/metabolism; Penicillin-Binding Proteins; Peptides/metabolism; Peptidyl Transferases; Streptomyces/enzymology; Substrate Specificity; Sulfhydryl Compounds/metabolism
Abstract :
[en] The Streptomyces K15 transferase is a penicillin-binding protein presumed to be involved in bacterial wall peptidoglycan crosslinking. It catalyses cleavage of the peptide, thiol ester or ester bond of carbonyl donors Z-R1-CONH-CHR2-COX-CHR3-COO- (where X is NH, S or O) and transfers the electrophilic group Z-R1-CONH-CHR2-CO to amino acceptors via an acyl-enzyme intermediate. Kinetic data suggest that the amino acceptor behaves as a simple alternative nucleophile at the level of the acyl-enzyme in the case of thiol ester and ester donors, and that it binds to the enzyme.carbonyl donor Michaelis complex and influences the rate of enzyme acylation by the carbonyl donor in the case of amide donors. Depending on the nature of the scissile bond, the enzyme has different requirements for substituents at positions R1, R2 and R3.
Research center :
CIP - Centre d'Ingénierie des Protéines - ULiège
Disciplines :
Microbiology
Biochemistry, biophysics & molecular biology
Author, co-author :
Grandchamps, Jacqueline;  Université de Liège - ULiège > Institut de Chimie > Centre d'Ingéniérie des Protéines
Nguyen-Distèche, Martine ;  Université de Liège - ULiège > Institut de Chimie > Centre d'ingénierie des protéines
Damblon, Christian ;  Université de Liège - ULiège > Insitut de Chimie > Centre d'ingéniérie des Protéines > LabOratoire d'Enzymologie
Frère, Jean-Marie ;  Université de Liège - ULiège > Insitut de Chimie > Centre d'ingénierie des protéines
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Insitut de Chimie > Centre d'Ingéniérie des Protéines
Language :
English
Title :
Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions.
Publication date :
1995
Journal title :
Biochemical Journal
ISSN :
0264-6021
eISSN :
1470-8728
Publisher :
Portland Press, London, United Kingdom
Volume :
307
Issue :
Pt 2
Pages :
335-339
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRSM - Fonds de la Recherche Scientifique Médicale [BE]
Available on ORBi :
since 27 November 2010

Statistics


Number of views
57 (5 by ULiège)
Number of downloads
134 (5 by ULiège)

Scopus citations®
 
20
Scopus citations®
without self-citations
12
OpenCitations
 
13

Bibliography


Similar publications



Contact ORBi