Home LiteratureArticle Details

PMID: 1059132 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 72 ·No. 9 ·1975-09-00 ·Pages 3463-7

Hammarström S, Strominger JL

Abstract

D-Alanine carboxypeptidase from Bacillus stearothermophilus is a membrane-bound enzyme which is inhibited by covalent interaction with penicillin G. The penicilloyl enzyme spontaneously reactivates and simultaneously releases a penicillin G degradation product; 0.2 mumol of the latter was isolated after incubation of 4.2 mumol of [8-14C]penicillin G with 10 g of membrane protein. It was identified as phenylacetylglycine by chromatographic techniques, infrared spectroscopy, and mass spectrometry. A mechanism for the degradation is proposed in which the remaining part of penicillin G would be released as 5,5-dimethyl-delta2-thiazoline-4-carboxylic acid. The implications of this finding are discussed.

MeSH Terms

Alanine Carboxypeptidases/metabolism Geobacillus stearothermophilus/enzymology Models, Biological Penicillin G/metabolism

Chemicals

Carboxypeptidases Alanine Penicillin G

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Hammarström S

Strominger J L

References (12)

12 references, click to expand

[Relation between arcus lipoides of the cornea and arteriosclerosis. Comparative studies based on 500 surgical cases].
Klin Wochenschr. 1967 Oct 15;45(20):1017-20 PMID: 5594034
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes.
Bacteriol Rev. 1974 Sep;38(3):291-335 PMID: 4608953
Penicillin-sensitive enzymes and penicillin-binding components in bacterial cells.
Ann N Y Acad Sci. 1974 May 10;235(0):210-24 PMID: 4277601
Biosynthesis of the peptidoglycan of bacterial cell walls. XV. The binding of radioactive penicillin to the particulate enzyme preparation of Bacillus subtilis and its reversal with hydroxylamine or thiols.
J Biol Chem. 1970 Jul 25;245(14):3653-9 PMID: 4248524
Five penicillin-binding components occur in Bacillus subtilis membranes.
J Biol Chem. 1972 Dec 25;247(24):8107-13 PMID: 4344991
Binding of (14C)penicillin G to the membrane-bound and the purified D-alanine carboxypeptidases from Bacillus stearothermophilus and Bacillus subtilis and its release.
J Biol Chem. 1974 Nov 10;249(21):6828-35 PMID: 4214007
Purification and characterization of the thermophilic D-alanine carboxypeptidase from membranes of Bacillus stearothermophilus.
J Biol Chem. 1974 Aug 10;249(15):4863-71 PMID: 4211099
D-alanine carboxypeptidase from Bacillus subtilis membranes. II. Interaction with penicillins and cephalosporins.
J Biol Chem. 1973 Oct 10;248(19):6767-71 PMID: 4200865
D-alanine carboxypeptidase from Bacillus subtilis membranes. I. Purification and characterization.
J Biol Chem. 1973 Oct 10;248(19):6759-66 PMID: 4200864
Degradation of penicillin G methyl ester with trifluoracetic acid.
J Org Chem. 1972 Aug 25;37(17):2733-5 PMID: 5054513
Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.
Proc Natl Acad Sci U S A. 1965 Oct;54(4):1133-41 PMID: 5219821

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.72.9.3463

Published

1975-09-00

Pages

3463-7

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC433014

Subset

External Links

PubMed source DOI: 10.1073/pnas.72.9.3463 PMC Full Text View journal details

Analysis Services

Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus.

Contact

WeChat Official Account