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ENZYME entry: EC 1.14.18.6

Accepted Name
4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase.
Reaction catalysed
  • an N-(1,2 saturated acyl)-(4R)-hydroxysphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 <=> an N-(2R-hydroxyacyl)-4R-hydroxysphinganine + 2 Fe(III)-[cytochrome b5] + H2O
  • an N-(1,2 saturated very-long-chain fatty acyl)-(R)-4-hydroxysphingoid base + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 <=> an N-(2R-hydroxy-very-long-chain fatty acyl)-(R)-4-hydroxysphingoid base + 2 Fe(III)-[cytochrome b5] + H2O
Comment(s)
  • 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 1.14.18.7.
Cross-references
BRENDA1.14.18.6
EC2PDB1.14.18.6
ExplorEnz1.14.18.6
PRIAM enzyme-specific profiles1.14.18.6
KEGG Ligand Database for Enzyme Nomenclature1.14.18.6
IUBMB Enzyme Nomenclature1.14.18.6
IntEnz1.14.18.6
MEDLINEFind literature relating to 1.14.18.6
MetaCyc1.14.18.6
Rhea expert-curated reactions1.14.18.6
UniProtKB/Swiss-Prot
Q03529, SCS7_YEAST

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