The active-site-serine penicillin-recognizing enzymes as members of the <i>Streptomyces</i> R61 <scp>dd</scp>-peptidase family

DOI PDF 被引用文献3件
  • B Joris
    Service de Microbiologie, Université de Liège, Institut de Chimie, B6, B-4000 Sart Tilman (Liège 1), Belgium.
  • J M Ghuysen
    Service de Microbiologie, Université de Liège, Institut de Chimie, B6, B-4000 Sart Tilman (Liège 1), Belgium.
  • G Dive
    Service de Microbiologie, Université de Liège, Institut de Chimie, B6, B-4000 Sart Tilman (Liège 1), Belgium.
  • A Renard
    Eurogentec S.A., Campus du Sart Tilman, B6 Bldg, B-4000 Liege, Belgium
  • O Dideberg
    Service de Cristallographie, Université de Liège, Institut de Physique, B5, B-4000 Sart Tilman (Liège 1), Belgium
  • P Charlier
    Service de Cristallographie, Université de Liège, Institut de Physique, B5, B-4000 Sart Tilman (Liège 1), Belgium
  • J M Frère
    Service de Microbiologie, Université de Liège, Institut de Chimie, B6, B-4000 Sart Tilman (Liège 1), Belgium.
  • J A Kelly
    Institute of Materials Science, Department of Molecular and Cell Biology, University of Connecticut, Storrs, CN 06268, U.S.A.
  • J C Boyington
    Institute of Materials Science, Department of Molecular and Cell Biology, University of Connecticut, Storrs, CN 06268, U.S.A.
  • P C Moews
    Institute of Materials Science, Department of Molecular and Cell Biology, University of Connecticut, Storrs, CN 06268, U.S.A.

書誌事項

公開日
1988-03-01
DOI
  • 10.1042/bj2500313
公開者
Portland Press Ltd.

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<jats:p>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.</jats:p>

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