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PMID: 2505721 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath).

Archives of microbiology ·Vol. 152 ·No. 2 ·1989-00-00 ·Pages 154-9

Stainthorpe AC, Murrell JC, Salmond GP, Dalton H, Lees V

Abstract

Methane monooxygenase (MMO) is the enzyme responsible for the conversion of methane to methanol in methanotrophic bacteria. In addition, this enzyme complex oxidizes a wide range of aliphatic and aromatic compounds in a number of potentially useful biotransformations. In this study, we have used biochemical data obtained from purification and characterization of the soluble MMO from Methylococcus capsulatus (Bath), to identify structural genes encoding this enzyme by oligonucleotide probing. The genes encoding the beta and gamma subunits of MMO were found to be chromosomally located and were linked in this organism. We report here on the analysis of a recombinant plasmid containing 12 kilobases of Methylococcus DNA and provide the first evidence for the localization and linkage of genes encoding the methane monooxygenase enzyme complex. DNA sequence analysis suggests that the primary structures of the beta and gamma subunits of MMO are completely novel and the complete sequence of these genes is presented.

MeSH Terms
Amino Acid Sequence Base Sequence Blotting, Southern Cloning, Molecular DNA, Bacterial/genetics Methylococcaceae/enzymology,genetics Molecular Sequence Data Oligonucleotide Probes Oxygenases/genetics Restriction Mapping
Chemicals
DNA, Bacterial Oligonucleotide Probes Oxygenases methane monooxygenase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Stainthorpe A C
Department of Biological Sciences, University of Warwick, Coventry, UK.
Murrell J C
Salmond G P
Dalton H
Lees V
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Article Info
Journal
Archives of microbiology
Abbr.
Arch Microbiol
ISSN
0302-8933
DOI
10.1007/BF00456094
Published
1989-00-00
Pages
154-9
Language
English
Region
Germany
NLM ID
0410427
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00456094 View journal details
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