Some properties of a D-alanine carboxypeptidase in envelope fractions of Neisseria gonorrhoeae.

Infection and immunity ·Vol. 12 ·No. 5 ·1975-11-00 ·Pages 1065-9

Davis RH, Salton MR

Abstract

Envelope preparations of Neisseria gonorrhoeae strain GC1 (a stable, piliated strain of intermediate colony morphology) and type T1 possess a D-alanine carboxypeptidase which releases the terminal alanine residue from the uridine 5'-diphosphate-N-acetyl muramylpentapeptide substrate (isolated from Bacillus cereus T). The D-alanine carboxypeptidase of the GC1 envelopes has a broad pH optimum between pH 8.0 to 10.0. When the molarity of the tris(hydroxymethyl)aminomethane buffer was varied, the activity showed an optimum over the range 0.2 to 0.4 M. Activity was higher (135% of control level) when 20 to 80 mM Mg2+ was present. The Km for the enzyme was 0.25 mM. The D-alanine carboxypeptidase was inhibited by several beta-lactam antibiotics and the 50% inhibitory levels were 10(-8) M penicillin G, 10(-8) M ampicillin, 10(-5) M cloxacillin, and 5 x 10(-7) M methicillin.

MeSH Terms

Carboxypeptidases/analysis,antagonists & inhibitors Cell Membrane/analysis Hydrogen-Ion Concentration Kinetics Muramoylpentapeptide Carboxypeptidase/analysis Neisseria gonorrhoeae/enzymology Penicillin G/pharmacology

Chemicals

Carboxypeptidases Muramoylpentapeptide Carboxypeptidase Penicillin G

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Davis R H

Salton M R

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18 references, click to expand

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Article Info

Journal

Infection and immunity

Abbr.

Infect Immun

ISSN

0019-9567

DOI

10.1128/iai.12.5.1065-1069.1975

Published

1975-11-00

Pages

1065-9

Language

English

Region

United States

NLM ID

0246127

PMCID

PMC415398

Subset

External Links

PubMed source DOI: 10.1128/iai.12.5.1065-1069.1975 PMC Full Text View journal details

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Some properties of a D-alanine carboxypeptidase in envelope fractions of Neisseria gonorrhoeae.

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