Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae

Lepage, S. ; Dubois, P. ; Ghosh, T. K. ; Joris, B. ; Mahapatra, S. ; Kundu, M. ; Basu, J. ; Chakrabarti, P. ; Cole, S. T. ; Nguyen-Disteche, M. ; Ghuysen, J. M. (1997) Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae Journal of Bacteriology, 179 (14). pp. 4627-4630. ISSN 0021-9193

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Official URL: http://jb.asm.org/cgi/content/abstract/179/14/4627

Abstract

The ponA gene of cosmid L222 of the Mycobacterium leprae genome library encodes a multimodular class A penicillin-binding protein (PBP), PBP1. The PBP, labelled with a polyhistidine sequence, has been produced in Escherichia coli, extracted from the membranes with 3-[(3- cholamidopropyl)-dimethylammonio]-1-propane-sulfonate (CHAPS) and purified by Ni2(+)-nitrilotriacetic acid-agarose chromatography. In contrast to the pon1-encoded class A PBP1, PBP1 undergoes denaturation at temperatures higher than 25 degrees C, it catalyzes acyl transfer reactions on properly structured thiolesters, and it binds penicillin with high affinity.

Item Type:Article
Source:Copyright of this article belongs to American Society for Microbiology.
ID Code:1523
Deposited On:05 Oct 2010 06:41
Last Modified:16 May 2016 12:38

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