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PMID: 7305936 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39.

The Biochemical journal ·Vol. 193 ·No. 1 ·1981-01-01 ·Pages 83-6

Duez C, Joris B, Frère JM, Ghuysen JM, Van Beeumen J

Abstract

Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu-Pro-Ala-Ser-Asn-Gly-Val-OH, where the benzylpenicilloyl group is ester-linked to the serine residue. This linkage is very labile and its hydrolysis causes the release of benzylpenicilloate. In contrast, the native benzylpenicilloyl-enzyme complex is very stable (half-life 70 h at 37 degrees C) and its breakdown proceeds via fragmentation of the bound benzylpenicilloyl group [Fuad, Frère, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623-629].

MeSH Terms

Amino Acid Sequence Benzeneacetamides Binding Sites Carboxypeptidases Electrophoresis Hot Temperature Muramoylpentapeptide Carboxypeptidase Nocardiaceae/enzymology Oligopeptides Penicillin G/analogs & derivatives Peptide Fragments/analysis Protein Denaturation Trypsin

Chemicals

Benzeneacetamides Oligopeptides Peptide Fragments benzylpenicilloyl-heptapeptide Carboxypeptidases Muramoylpentapeptide Carboxypeptidase Trypsin Penicillin G

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Duez C

Joris B

Frère J M

Ghuysen J M

Van Beeumen J

References (14)

14 references, click to expand

Chemical studies on methionyl-tRNA synthetase from Escherichia coli.
J Mol Biol. 1970 Sep 14;52(2):165-78 PMID: 4922213
Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis.
J Biol Chem. 1972 May 25;247(10):3242-51 PMID: 4112808
Sequence analysis of fluorescamine-stained peptides and proteins purified on a nanomole scale. Application to proteins of bacteriophage MS2.
Eur J Biochem. 1974 May 2;44(1):279-88 PMID: 4854242
Binding of beta-lactam antibiotics to the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.
Biochem J. 1974 Oct;143(1):241-9 PMID: 4464853
Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39.
Nature. 1975 Nov 13;258(5531):168-70 PMID: 1186898
Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61.
Nature. 1976 Apr 1;260(5550):451-4 PMID: 815828
Beta-lactamase inactivation by mechanism-based reagents.
Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):309-19 PMID: 6109326
Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxy-peptidase-transpeptidase from Streptomyces R61.
FEBS Lett. 1976 Nov;70(1):257-60 PMID: 992070
Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of Bacillus subtilis.
Proc Natl Acad Sci U S A. 1977 Mar;74(3):1009-12 PMID: 403523
NMR evidence for the structure of the complex between penicillin and the DD-carboxypeptidase of Streptomyces R61.
FEBS Lett. 1979 Feb 1;98(1):53-6 PMID: 428542
Penicillinase active sites: labelling of serine-44 in beta-lactamase I by 6beta-bromopenicillanic acid.
FEBS Lett. 1979 Mar 1;99(1):59-61 PMID: 220094
Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.
Proc Natl Acad Sci U S A. 1979 Jun;76(6):2730-4 PMID: 111240
Use of model enzymes in the determination of the mode of action of penicillins and delta 3-cephalosporins.
Annu Rev Biochem. 1979;48:73-101 PMID: 112913
Mode of interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidase--transpeptidase from Streptomyces R39.
Biochem J. 1976 Jun 1;155(3):623-9 PMID: 949323

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1930083

Published

1981-01-01

Pages

83-6

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1162578

Subset

Grants

NIAID NIH HHS · AI13364-04 · United States

External Links

PubMed source DOI: 10.1042/bj1930083 PMC Full Text View journal details

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The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39.

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