PMID: 6976797Jan 4, 1982Paper

Purification and properties of the exocellular beta-lactamase of Actinomadura strain R39

Biochimica Et Biophysica Acta
C DuezL Dierickx

Abstract

The exocellular beta-lactamase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) of Actinomadura R39 consists of one single polypeptide chain of molecular weight about 15 200. It exhibits a highly asymmetrical shape, has a low isoelectric point (at pH 5.0) and contains about 9.3% (w/w) of a polydeoxyribonucleotide with which it forms a rather stable complex. Removal of a substantial amount of this deoxyribonucleotide by treatment with DNAase I has no effect on the enzyme activity. The beta-lactamase has a wide spectrum of activity. Penicillins and delta 3-cephalosporins can be either good or poor substrates. Oxacillin, which is a poor substrate of most beta-lactamases from Gram-positive bacteria, is a good substrate of the beta-lactamase of Actinomadura R39. Its best substrate, however, is nitrocefin (kcat/Km: 2300 000 M-1.s-1; catalytic centre activity: 210 s-1). The kcat/Km values observed with some penicillins and delta 3-cephalosporins are similar to the values of the bimolecular rate constants that govern the formation of the acyl-enzyme intermediates between these antibiotics and the serine D-alanyl-D-alanine peptidase that is also secreted by the same strain Actinomadura R39. Such a relationship, however, is not observ...Continue Reading

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Citations

Jan 1, 1985·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·M CamposP Ward
Mar 1, 1989·Antimicrobial Agents and Chemotherapy·K Bush
Jun 1, 1995·Antimicrobial Agents and Chemotherapy·K BushA A Medeiros
Mar 12, 2010·Protein Engineering, Design & Selection : PEDS·Girja S Shukla, David N Krag
Jan 1, 1985·Biotechnology & Genetic Engineering Reviews·A Coulson
Feb 8, 2007·International Journal of Cancer. Journal International Du Cancer·Girja S ShuklaDavid N Krag
Jan 1, 1985·Critical Reviews in Microbiology·J M Frère, B Joris

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