The active sites of the beta-lactamases of Streptomyces cacaoi and Streptomyces albus G

Biochem J. 1987 Jun 1;244(2):427-32. doi: 10.1042/bj2440427.

Abstract

The active-site serine of the extracellular beta-lactamases of Streptomyces cacaoi and Streptomyces albus G has been labelled with beta-iodopenicillanate. The determination of the sequence of the labelled peptides obtained after trypsin digestion of the denatured proteins indicate both enzymes to be class A beta-lactamases. Surprisingly the two Streptomyces enzymes do not appear to be especially homologous, and none of them exhibited a high degree of homology with the Streptomyces R61 DD-peptidase. Our data confirm that, as a family of homologous enzymes, class A is rather heterogeneous, with only a small number of conserved residues in all members of the class.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Chromatography, Ion Exchange
  • Dithionitrobenzoic Acid / pharmacology
  • Mercaptoethanol / pharmacology
  • Penicillanic Acid / pharmacology
  • Peptide Fragments / isolation & purification
  • Spectrophotometry, Ultraviolet
  • Streptomyces / enzymology*
  • beta-Lactamases / metabolism*

Substances

  • Peptide Fragments
  • Mercaptoethanol
  • Penicillanic Acid
  • Dithionitrobenzoic Acid
  • 6-iodopenicillanic acid
  • beta-Lactamases