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PMID: 2400398 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Chromogenic depsipeptide substrates for beta-lactamases and penicillin-sensitive DD-peptidases.

The Biochemical journal ·Vol. 270 ·No. 2 ·1990-09-01 ·Pages 525-9

Adam M, Damblon C, Plaitin B, Christiaens L, Frère JM

Abstract

Various ester and thioester derivatives of hippuric acid have been prepared which were substrates of both beta-lactamases and DD-peptidases. The thioesters were more rapidly hydrolysed by nearly all the enzymes. Surprisingly, the enzymes acted rather efficiently on substrates which did not contain any chiral centre.

MeSH Terms
Amino Acid Sequence Chromogenic Compounds/metabolism Esters Hydrolysis Kinetics Molecular Sequence Data Molecular Structure Muramoylpentapeptide Carboxypeptidase/metabolism Oligopeptides/metabolism Penicillins/pharmacology Pronase/metabolism Substrate Specificity beta-Lactamases/metabolism
Chemicals
Chromogenic Compounds Esters Oligopeptides Penicillins Muramoylpentapeptide Carboxypeptidase Pronase beta-Lactamases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Adam M
Laboratoire d'Enzymologie, Université de Liĕge, Sart Tilman, Belgium.
Damblon C
Plaitin B
Christiaens L
Frère J M
References (9)
9 references, click to expand
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    Biochem J. 1986 Aug 15;238(1):309-12 PMID: 3800940
  7. Automated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases.
    Biochem Pharmacol. 1987 Jul 15;36(14):2393-403 PMID: 3038122
  8. Kinetics and mechanism of the serine beta-lactamase catalyzed hydrolysis of depsipeptides.
    Biochemistry. 1987 Jun 16;26(12):3385-95 PMID: 3115289
  9. The diversity of the catalytic properties of class A beta-lactamases.
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1990-09-01
Pages
525-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1131754
Subset
IM
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