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ENZYME entry: EC

Accepted Name
4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase.
Reaction catalysed
A phytoceramide + 2 ferrocytochrome b5 + O(2) + 2 H(+) <=> a (2'R)-2'-hydroxyphytoceramide + 2 ferricytochrome b5 + H(2)O
  • The enzyme, characterized from yeast and mammals, catalyzes the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis.
  • The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site.
  • The newly introduced 2-hydroxyl group has R-configuration.
  • Cf. EC
PRIAM enzyme-specific profiles1.14.18.6
KEGG Ligand Database for Enzyme Nomenclature1.14.18.6
IUBMB Enzyme Nomenclature1.14.18.6
MEDLINEFind literature relating to

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.18.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-