Reference : Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptid...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Microbiology
http://hdl.handle.net/2268/77930
Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions.
English
Grandchamps, Jacqueline [Université de Liège - ULg > Institut de Chimie > > Centre d'Ingéniérie des Protéines > >]
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des protéines > >]
Damblon, Christian mailto [Université de Liège - ULg > Insitut de Chimie > Centre d'ingéniérie des Protéines > LabOratoire d'Enzymologie > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Insitut de Chimie > Centre d'ingénierie des protéines > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Insitut de Chimie > Centre d'Ingéniérie des Protéines > > > >]
1995
Biochemical Journal
Portland Press
307
Pt 2
335-339
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] 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
[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.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/77930
http://www.biochemj.org/bj/default.htm
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