Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b.
The oxidation of methane to methanol in methanotrophic bacteria is catalysed by the enzyme methane monooxygenase (MM0). This multicomponent enzyme catalyses a range of oxidations including that of aliphatic and aromatic compounds and therefore has potential for commercial exploitation. This study details the molecular characterization of the soluble MMO (sMMO) genes from the Type II methanotroph Methylosinus trichosporium OB3b. The structural genes encoding the alpha, beta and gamma subunits of sMMO protein A and the structural gene encoding component B have been isolated and sequenced. These genes have been expressed and their products identified using an in vitro system. A comparative analysis of sMMO predicted sequences of M. trichosporium OB3b and the taxonomically related M. capsulatus (Bath) is also presented.
Cardy
D L
DL
Department of Biological Sciences, University of Warwick, Coventry, UK.
Laidler
V
V
Salmond
G P
GP
Murrell
J C
JC
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D005798:Genes, Bacterial; D008772:Methylococcaceae / Q000235:genetics*; D008969:Molecular Sequence Data; D005810:Multigene Family; D010105:Oxygenases / Q000235:genetics* / Q000378:metabolism; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D012995:Solubility
D004269:DNA, Bacterial; D010105:Oxygenases; C021555:methane monooxygenase