| 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 19383682] |
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| [EC 1.14.13.230 created 2016] |
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