Purification and partial characterization of a penicillin-binding protein from Mycobacterium smegmatis.

Abstract:

:Penicillin-binding proteins (PBPs), although characterized from several organisms, have so far not been studied in mycobacteria. The present study is the first characterization of a PBP from Mycobacterium smegmatis. The PBP was purified by solubilization of the membranes with Triton X-100 and successive chromatography of the solubilized proteins on ampicillin-linked CH Sepharose 4B and DE-52. The purified PBP (M(r), 49,500) catalyzed a model transpeptidase reaction with the tripeptide acetyl2-L-Lys-D-Ala-D-Ala as the substrate and Gly-Gly as the acceptor. The transpeptidase activity was inhibited by 50% at a benzylpenicillin concentration of 1.8 x 10(-7) M, which was similar to the concentration (1.1 x 10(-7) M) of benzylpenicillin required to saturate to 50% this PBP. Of several antibiotics tested, the concentration of antibiotic required to inhibit [35S]penicillin binding by 90% was found to be the lowest for cefoxitin and Sch 34343.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Basu J,Chattopadhyay R,Kundu M,Chakrabarti P

doi

10.1128/jb.174.14.4829-4832.1992

keywords:

subject

Has Abstract

pub_date

1992-07-01 00:00:00

pages

4829-32

issue

14

eissn

0021-9193

issn

1098-5530

journal_volume

174

pub_type

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