The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 dd-peptidase family

Biochemical Journal - Tập 250 Số 2 - Trang 313-324 - 1988
Bernard Joris1, Jean‐Marie Ghuysen1, Georges Dive1, A. Renard2, Andréa Dessen3, P. Charlier3, Jean‐Marie Frère1, Julia Kelly4, Jeffrey C. Boyington4, P. C. Moews4
1Service de Microbiologie, Université de Liège, Institut de Chimie, B6, B-4000 Sart Tilman (Liège 1), Belgium
2Eurogentec S.A., Campus du Sart Tilman, B6 Bldg, B-4000 Liege, Belgium
3Service de Cristallographie, Université de Liège, Institut de Physique, B5, B-4000 Sart Tilman (Liège 1), Belgium
4Institute of Materials Science, Department of Molecular and Cell Biology, University of Connecticut, Storrs, CN 06268, U.S.A.

Tóm tắt

Homology searches and amino acid alignments, using the Streptomyces R61 DD-peptidase/penicillin-binding protein as reference, have been applied to the beta-lactamases of classes A and C, the Oxa-2 beta-lactamase (considered as the first known member of an additional class D), the low-Mr DD-peptidases/penicillin-binding proteins (protein no. 5 of Escherichia coli and Bacillus subtilis) and penicillin-binding domains of the high-Mr penicillin-binding proteins (PBP1A, PBP1B, PBP2 and PBP3 of E. coli). Though the evolutionary distance may vary considerably, all these penicillin-interactive proteins and domains appear to be members of a single superfamily of active-site-serine enzymes distinct from the classical trypsin or subtilisin families. The amino acid alignments reveal several conserved boxes that consist of strict identities or homologous amino acids. The significance of these boxes is highlighted by the known results of X-ray crystallography, chemical derivatization and site-directed-mutagenesis experiments.

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Biochemical Journal

Tập 250 Số 2

313-324

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