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ENZYME

ENZYME entry: EC 1.2.1.84

Accepted Name
alcohol-forming fatty acyl-CoA reductase
Reaction catalysed
a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH <=> a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Comment(s)
  • The enzyme has been characterized from the plant Simmondsia chinensis (jojoba).
  • The alcohol is formed by a four-electron reduction of fatty acyl-CoA.
  • Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released.
  • The recombinant enzyme was shown to accept saturated and mono- unsaturated fatty acyl-CoAs of 16 to 22 carbons.
Cross-references
BRENDA1.2.1.84
EC2PDB1.2.1.84
ExplorEnz1.2.1.84
PRIAM enzyme-specific profiles1.2.1.84
KEGG Ligand Database for Enzyme Nomenclature1.2.1.84
IUBMB Enzyme Nomenclature1.2.1.84
IntEnz1.2.1.84
MEDLINEFind literature relating to 1.2.1.84
MetaCyc1.2.1.84
Rhea expert-curated reactions1.2.1.84
UniProtKB/Swiss-Prot
Q39152, FACR1_ARATHQ5ZM72, FACR1_CHICKA1ZAI5, FACR1_DROME
Q8WVX9, FACR1_HUMANQ922J9, FACR1_MOUSEQ5R834, FACR1_PONAB
Q66H50, FACR1_RATQ7ZXF5, FACR1_XENLAQ08891, FACR2_ARATH
Q0P5J1, FACR2_BOVINA1ZAI3, FACR2_DROMEQ96K12, FACR2_HUMAN
Q7TNT2, FACR2_MOUSEQ93ZB9, FACR3_ARATHQ960W6, FACR3_DROME
Q9LXN3, FACR4_ARATHQ0WRB0, FACR5_ARATHB9TSP7, FACR6_ARATH
Q1PEI6, FACR8_ARATHQ9XGY7, FAR_SIMCHQ8MS59, WAT_DROME

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.2.1.-
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