Purification of isopenicillin N synthetase

Biochem J. 1984 Sep 15;222(3):789-95. doi: 10.1042/bj2220789.

Abstract

Isopenicillin N synthetase was extracted from Cephalosporium acremonium and purified about 200-fold. The product showed one major protein band, coinciding with synthetase activity, when subjected to electrophoresis in polyacrylamide gel. An isopenicillin N synthetase from Penicillium chrysogenum was purified about 70-fold by similar procedures. The two enzymes resemble each other closely in their Mr, in their mobility on electrophoresis in polyacrylamide gel and in their requirement for Fe2+ and ascorbate for maximum activity. Preliminary experiments have shown that a similar isopenicillin N synthetase can be extracted from Streptomyces clavuligerus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acremonium / enzymology
  • Chromatography, Affinity
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Enzymes / isolation & purification*
  • Oxidoreductases*
  • Penicillium chrysogenum / enzymology
  • Streptomyces / enzymology

Substances

  • Enzymes
  • Oxidoreductases
  • isopenicillin N synthetase