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

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

doi:10.1007/BF00305358

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

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

Imperial College London

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	231-234
Number of pages	4
Journal	Archives of Microbiology
Volume	163
Issue number	3
DOIs	https://doi.org/10.1007/BF00305358
Publication status	Published - 1 Mar 1995

Keywords

C-Radiolabelling
Mycobacterium sp.
Propene monooxygenase

ASJC Scopus subject areas

Microbiology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/BF00305358

Cite this

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title = "Properties of a soluble propene monooxygenase from Mycobacterium sp. (strain M156)",

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.",

keywords = "C-Radiolabelling, Mycobacterium sp., Propene monooxygenase",

author = "Woodland, {Marc P.} and Matthews, {Colette S.} and Leak, {David J.}",

year = "1995",

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doi = "10.1007/BF00305358",

language = "English",

volume = "163",

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T1 - Properties of a soluble propene monooxygenase from Mycobacterium sp. (strain M156)

AU - Woodland, Marc P.

AU - Matthews, Colette S.

AU - Leak, David J.

PY - 1995/3/1

Y1 - 1995/3/1

N2 - 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.

AB - 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.

KW - C-Radiolabelling

KW - Mycobacterium sp.

KW - Propene monooxygenase

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U2 - 10.1007/BF00305358

DO - 10.1007/BF00305358

M3 - Article

AN - SCOPUS:0028934666

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VL - 163

SP - 231

EP - 234

JO - Archives of Microbiology

JF - Archives of Microbiology

IS - 3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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