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. 1997 Jul;179(14):4627-30.
doi: 10.1128/jb.179.14.4627-4630.1997.

Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae

S Lepage  1 , P Dubois, T K Ghosh, B Joris, S Mahapatra, M Kundu, J Basu, P Chakrabarti, S T Cole, M Nguyen-Distèche, J M Ghuysen
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Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae

S Lepage et al. J Bacteriol. 1997 Jul.

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.

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