Jump to content

Alkane 1-monooxygenase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Dcirovic (talk | contribs) at 09:23, 31 December 2015 (added link to portal). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

alkane 1-monooxygenase
Identifiers
EC no.1.14.15.3
CAS no.9059-16-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, an alkane 1-monooxygenase (EC 1.14.15.3) is an enzyme that catalyzes the chemical reactions

an alkane + reduced rubredoxin + O2 a primary alcohol + oxidized rubredoxin + H2O.

Alkanes of 6 to 22 carbons have been observed as substrates.[1] This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with oxygen as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is alkane, reduced-rubredoxin:oxygen 1-oxidoreductase. Other names in common use include alkane 1-hydroxylase, omega-hydroxylase, fatty acid omega-hydroxylase, alkane monooxygenase, 1-hydroxylase, AlkB, and alkane hydroxylase. It contains a diiron non-heme active site.

References

  1. ^ McKenna EJ, Coon MJ (1970). "Enzymatic omega-oxidation. IV. Purification and properties of the omega-hydroxylase of Pseudomonas oleovorans". J. Biol. Chem. 245 (15): 3882–9. PMID 4395379.
  • Cardini G, Jurtshuk P (1970). "The enzymatic hydroxylation of n-octane by Corynebacterium sp strain 7E1C". J. Biol. Chem. 245 (11): 2789–96. PMID 4317878.
  • Peterson JA, Kusunose M, Kusunose E, Coon MJ (1967). "Enzymatic omega-oxidation. II. Function of rubredoxin as the electron carrier in omega-hydroxylation". J. Biol. Chem. 242 (19): 4334–40. PMID 4294330.{{cite journal}}: CS1 maint: multiple names: authors list (link)