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

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

Research output: Contribution to journalArticle

Abstract

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
Volume163
Issue number3
DOIs
Publication statusPublished - 1 Mar 1995

Keywords

  • C-Radiolabelling
  • Mycobacterium sp.
  • Propene monooxygenase

ASJC Scopus subject areas

  • Microbiology

Cite this

Properties of a soluble propene monooxygenase from Mycobacterium sp. (strain M156). / Woodland, Marc P.; Matthews, Colette S.; Leak, David J.

In: Archives of Microbiology, Vol. 163, No. 3, 01.03.1995, p. 231-234.

Research output: Contribution to journalArticle

Woodland, Marc P. ; Matthews, Colette S. ; Leak, David J. / Properties of a soluble propene monooxygenase from Mycobacterium sp. (strain M156). In: Archives of Microbiology. 1995 ; Vol. 163, No. 3. pp. 231-234.
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