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Information on EC - 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase

for references in articles please use BRENDA:EC1.14.18.6
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IUBMB Comments
The enzyme, characterized from yeast and mammals, catalyses 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, dihydroceramide fatty acyl 2-hydroxylase.
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The enzyme appears in viruses and cellular organisms
fa2h, fatty acid 2-hydroxylase, atfah1, fatty acid alpha-hydroxylase, scs7p, sphingolipid alpha-hydroxylase, fatty acid 2-hydroxylase 1, more
a phytoceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (2'R)-2'-hydroxyphytoceramide + 2 ferricytochrome b5 + H2O
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