Properties of a soluble propene monooxygenase from Mycobacterium sp. (strain M156)

Marc P. Woodland, Colette S. Matthews, David J. Leak

Research output: Contribution to journalArticlepeer-review


Mycobacterium sp. strain M156, isolated on propene as sole carbon and energy source, possessed NAD(P)H-linked propene monooxygenase (PMO) activity. The enzyme was soluble, unstable, and of low specific activity. Batch ion-exchange chromatography resolved the extracts into two fractions, both of which were essential for activity. Using 14C-acetylene as a suicide substrate, a single polypeptide was radiolabelled and subsequently purified to generate an N-terminal sequence. We suspect this polypeptide to be an integral part of the oxygenase enzyme component.

Original languageEnglish
Pages (from-to)231-234
Number of pages4
JournalArchives of Microbiology
Issue number3
Publication statusPublished - 1 Mar 1995


  • C-Radiolabelling
  • Mycobacterium sp.
  • Propene monooxygenase

ASJC Scopus subject areas

  • Microbiology


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