EC 1 - Oxidoreductases
EC 1.14 - Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O2
EC 1.14.15 - With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
EC 1.14.15.3 - Alkane 1-monooxygenase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.14.15.3
Names
Accepted name:
alkane 1-monooxygenase
Other
names:
1-hydroxylase
ω-hydroxylase
alkane 1-hydroxylase
alkane hydroxylase
alkane monooxygenase
fatty acid ω-hydroxylase
ω-hydroxylase
alkane 1-hydroxylase
alkane hydroxylase
alkane monooxygenase
fatty acid ω-hydroxylase
Systematic name:
alkane,reduced-rubredoxin:oxygen 1-oxidoreductase
Reaction
- octane + 2 reduced rubredoxin + O2 + 2 H+ = 1-octanol + 2 oxidized rubredoxin + H2O
Comments:
Some enzymes in this group are heme-thiolate proteins (P-450). Also hydroxylates fatty acids in the ω-position.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UM-BBD
,
UniPathway
Protein domains and families:
PROSITE:PDOC00081
Gene Ontology:
GO:0018685
,
GO:0052869
CAS Registry Number:
9059-16-9
UniProtKB/Swiss-Prot:
ALKB1_ALCBS
ALKB1_PSEAE
ALKB2_ALCBS
ALKB2_PSEAE
ALKB_ACIAD
ALKB_PSEOL
ALKB_PSEPU
References
-
The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C.J. Biol. Chem. 245 : 2789-2796 (1970). [PMID: 4317878]
-
Enzymatic ω-oxidation. IV. Purification and properties of the ω-hydroxylase of Pseudomonas oleovorans.J. Biol. Chem. 245 : 3882-3889 (1970). [PMID: 4395379]
-
Enzymatic ω-oxidation. II. Function of rubredoxin as the electron carrier in ω-hydroxylation.J. Biol. Chem. 242 : 4334-4340 (1967). [PMID: 4294330]
[EC 1.14.15.3 created 1972]