Dihydroceramide desaturase


Dihydroceramide desaturase is the enzyme involved in the conversion of dihydroceramide into ceramide by inserting the 4,5-trans-double bond to the sphingolipid backbone of dihydroceramide. DDase require the and the NAD(P)H as cofactor.
The activity of DDase is influenced by several factors as
  1. alkyl chain length of the sphingoid base and fatty acid
  2. The stereochemistry of the sphingoid base
  3. the nature of the headgroup, with the highest activity with dihydroceramide, but some activity with dihydrog lucosylceramide
  4. The ability to utilize alternative reductants like ascorbic acid could substitute for a reduced pyridine nucleotide, but it act as inhibitory at higher concentrations.
N-octanamide, is the inhibitor DDase activity.