EC Number   |
General Information |
Reference |
|---|
   1.14.19.13 | evolution |
all members of the CSFAD3 subclass contain eight exons and seven introns within the gene. Evolutionary relationship of Cannabis sativa putative desaturases, overview |
746012 |
| 1.14.19.13 | evolution |
bifunctional DELTA12/DELTA15-desaturases are widely found in fungi species belonging to Ascomycota and Basidiomycota. Enzyme RKD12 shares higher homology to the Cop-odeA, it only exhibits DELTA12 and DELTA15 desaturation activity on C18 substrates without preference |
-, 744576 |
| 1.14.19.13 | evolution |
three different copies of the genes FAD2 and FAD3 are identified, which contain three histidine rich motifs (HXCGHX, HRXHH andHVXHH) and six highly conserved transmembrane domains. Comparing their sequences, the CsFAD2copies accommodate four conservative changes (E36D, R48H, V97A, and A177P) and two semi-conservative ones (V63I and L249M), whereas only one semi-conservative change (A327S) is detected in CsFAD3 but with two extra amino acids (H147 and G148) |
745061 |
| 1.14.19.13 | metabolism |
the enzyme is is thought to be involved in 18:5n-3 biosynthesis |
-, 744387 |
| 1.14.19.13 | more |
hemp seeds contain three DELTA15 desaturases, FAD3A is the major DELAT15 desaturase in hemp seed |
746012 |
| 1.14.19.13 | more |
the enzyme contains a putative transit sequence for localization in chloroplasts and a DELTA6 desaturase-like domain, but it does not contain a cytochrome b5 domain nor typical His-boxes found in DELTA15 desaturases |
-, 744387 |
| 1.14.19.13 | physiological function |
DELTA12-fatty acid desaturase CpFAD2 from Candida parapsilosis is a multifunctional desaturase producing a range of DELTA12- and DELTA15-polyunsaturated and hydroxylated fatty acids |
-, 746264 |
| 1.14.19.13 | physiological function |
DELTA12-fatty acid desaturase CpFAD3 from Candida parapsilosis is a DELTA15-desaturase producing DELTA15-polyunsaturated fatty acids, i.e., alpha-linolenic acid (DELTA9,DELTA12,DELTA15-18:3) and hexadecatrienoic acid with an unusual terminal double bond (DELTA9,DELTA12,DELTA15-16:3), overview |
-, 746264 |
| 1.14.19.13 | physiological function |
for better adaptation to low temperatures, Rhodosporidium kratochvilovae YM25235 may have evolved some adaptative mechanisms that might include the alteration of unsaturation levels of fatty acids in membrane lipids involving the enzyme |
-, 744576 |
| 1.14.19.13 | physiological function |
the FAD3 enzyme is responsible for the DELTA15 desaturation of linoleic acid (18:2DELTA9,12) to alpha-linolenoic acid (18:3DELTA9,12,15) |
746012 |
