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. 1991 Oct 15;279(Pt 2):601–604. doi: 10.1042/bj2790601

Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteins.

M Adam 1, C Damblon 1, M Jamin 1, W Zorzi 1, V Dusart 1, M Galleni 1, A el Kharroubi 1, G Piras 1, B G Spratt 1, W Keck 1, et al.
PMCID: PMC1151646  PMID: 1953655

Abstract

The high-molecular-mass penicillin-binding proteins (HMM-PBPs), present in the cytoplasmic membranes of all eubacteria, are involved in important physiological events such as cell elongation, septation or shape determination. Up to now it has, however, been very difficult or impossible to study the catalytic properties of the HMM-PBPs in vitro. With simple substrates, we could demonstrate that several of these proteins could catalyse the hydrolysis of some thioesters or the transfer of their acyl moiety on the amino group of a suitable acceptor nucleophile. Many of the acyl-donor substrates were hippuric acid or benzoyl-D-alanine derivatives, and their spectroscopic properties enabled a direct monitoring of the enzymic reaction. In their presence, the binding of radioactive penicillin to the PBPs was also inhibited.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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