The Enzyme Database

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EC 1.14.13.230     
Accepted name: butane monooxygenase (soluble)
Reaction: butane + NADH + H+ + O2 = butan-1-ol + NAD+ + H2O
Other name(s): sBMO; bmoBCDXYZ (gene names)
Systematic name: butane,NADH:oxygen oxidoreductase
Comments: The enzyme, characterized from the bacterium Thauera butanivorans, is similar to EC 1.14.13.25, methane monooxygenase (soluble), but has a very low activity with methane. It comprises three components - a carboxylate-bridged non-heme di-iron center-containing hydroxylase (made of three different subunits), a flavo-iron sulfur-containing NADH-oxidoreductase, and a small regulatory component protein. The enzyme can also act on other C3-C6 linear and branched aliphatic alkanes with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sluis, M.K., Sayavedra-Soto, L.A. and Arp, D.J. Molecular analysis of the soluble butane monooxygenase from ’Pseudomonas butanovora’. Microbiology 148 (2002) 3617–3629. [PMID: 12427952]
2.  Dubbels, B.L., Sayavedra-Soto, L.A. and Arp, D.J. Butane monooxygenase of ’Pseudomonas butanovora’: purification and biochemical characterization of a terminal-alkane hydroxylating diiron monooxygenase. Microbiology 153 (2007) 1808–1816. [PMID: 17526838]
3.  Doughty, D.M., Kurth, E.G., Sayavedra-Soto, L.A., Arp, D.J. and Bottomley, P.J. Evidence for involvement of copper ions and redox state in regulation of butane monooxygenase in Pseudomonas butanovora. J. Bacteriol. 190 (2008) 2933–2938. [PMID: 18281403]
4.  Cooley, R.B., Dubbels, B.L., Sayavedra-Soto, L.A., Bottomley, P.J. and Arp, D.J. Kinetic characterization of the soluble butane monooxygenase from Thauera butanivorans, formerly ’Pseudomonas butanovora’. Microbiology 155 (2009) 2086–2096. [PMID: 19383682]
[EC 1.14.13.230 created 2016]
 
 


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