ID   1.14.19.17
DE   sphingolipid 4-desaturase.
AN   dehydroceramide desaturase.
CA   an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 =
CA   an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O.
CC   -!- The enzyme, which has been characterized from plants, fungi,
CC       and mammals, generates a trans double bond at position 4 of
CC       sphinganine bases in sphingolipids.
CC   -!- The preferred substrate is dihydroceramide, but the enzyme is also
CC       active with dihydroglucosylceramide.
CC   -!- Unlike EC 1.14.19.29, this enzyme does not contain an integral
CC       cytochrome b5 domain and requires an external cytochrome b5.
CC   -!- The product serves as an important signaling molecules in mammals and
CC       is required for spermatide differentiation.
DR   Q3ZBY7, DEGS1_BOVIN;  O44186, DEGS1_CAEEL;  Q5F3C1, DEGS1_CHICK;
DR   Q94515, DEGS1_DROME;  O15121, DEGS1_HUMAN;  Q6UQ04, DEGS1_MICFO;
DR   O09005, DEGS1_MOUSE;  Q5RE51, DEGS1_PONAB;  Q5XIF5, DEGS1_RAT  ;
DR   Q68FB8, DEGS1_XENTR;  Q0II71, DEGS2_BOVIN;  G5EC63, DEGS2_CAEEL;
DR   Q6QHC5, DEGS2_HUMAN;  Q8R2F2, DEGS2_MOUSE;  Q564G3, DEGS2_RAT  ;
DR   Q5AJX2, DEGS_CANAL ;  C4R613, DEGS_KOMPG ;  O59715, DEGS_SCHPO ;
DR   Q9ZPH4, DES1L_ARATH;  Q6H5U3, DES1L_ORYSJ;
//