| EC |
1.14.15.3 |
| Accepted name: |
alkane 1-monooxygenase |
| Reaction: |
octane + 2 reduced rubredoxin + O2 + 2 H+ = 1-octanol + 2 oxidized rubredoxin + H2O |
| Other name(s): |
alkane 1-hydroxylase; ω-hydroxylase; fatty acid ω-hydroxylase; alkane monooxygenase; 1-hydroxylase; alkane hydroxylase |
| Systematic name: |
alkane,reduced-rubredoxin:oxygen 1-oxidoreductase |
| Comments: |
Some enzymes in this group are heme-thiolate proteins (P-450). Also hydroxylates fatty acids in the ω-position. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9059-16-9 |
| References: |
| 1. |
Cardini, G. and Jurtshuk, P. The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C. J. Biol. Chem. 245 (1970) 2789–2796. [PMID: 4317878] |
| 2. |
McKenna, E.J. and Coon, M.J. Enzymatic ω-oxidation. IV. Purification and properties of the ω-hydroxylase of Pseudomonas oleovorans. J. Biol. Chem. 245 (1970) 3882–3889. [PMID: 4395379] |
| 3. |
Peterson, J.A., Kusunose, M., Kusunose, E. and Coon, M.J. Enzymatic ω-oxidation. II. Function of rubredoxin as the electron carrier in ω-hydroxylation. J. Biol. Chem. 242 (1967) 4334–4340. [PMID: 4294330] |
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| [EC 1.14.15.3 created 1972] |
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