EC Number   |
General Information |
Reference |
|---|
   1.14.18.6 | evolution |
FA2H/Scs7p belongs to a superfamily of integral membrane di-iron-containing enzymes that hydroxylate or desaturate lipid-based substrates via a reaction mechanism that is dependent on NADH and oxygen |
742884 |
| 1.14.18.6 | more |
important role of the dimetal-binding histidines in catalysis, residues Tyr322 and Asp323 are critical determinants involved in the hydroxylase reaction. Molecular dynamics simulations, structure-function analysis, and generation of a model of ceramide binding to enzyme Scs7p |
742884 |
| 1.14.18.6 | physiological function |
a yeast strain that lacks the FAH1 gene is resistant to antifungal cyclic lipodepsinonapeptide syringomycin E |
733851 |
| 1.14.18.6 | physiological function |
COS7 cells expressing human FA2H contain 3-20fold higher levels of 2-hydroxyceramides (C16, C18, C24, and C24:1) and 2-hydroxy fatty acids compared with control cells |
734146 |
| 1.14.18.6 | physiological function |
Deletion of hydroxylase scs7 causes synthetic lethality in combination deletion of phosphoinositide phosphatase SAC1. Overexpression of PSS1 encoding phosphatidylserine synthase complements the growth defects of scs7 deletion cells under SAC1-repressive conditions, and overexpression of Arf-GAP AGE1, which encodes aprotein related to membrane trafficking, also complements |
734709 |
| 1.14.18.6 | physiological function |
disruption of the FAH1 gene does not give any visible phenotype, and there is no observable difference in content or distribution of the most abundant long chain saturated and unsaturated 14-18-carbon fatty acid species. The gene-disrupted DELTAfah1 strain shows an approximately 40fold reduction of alpha-hydroxy-fatty acid 26:0 and a complementary increase in fatty acid 26:0. Expression of Arabidopsis thaliana FAH1 gene, which does not contain the cytochrome b5 domain, in the Saccharomyces cerevisiae DELTAfah1 strain produces an approximately 25fold increase in alpha-hydroxyfatty acid 26:0 and reduces the levels of its 26-carbon precursor |
734124 |
| 1.14.18.6 | physiological function |
enzyme Scs7p is responsible for adding a hydroxyl group to the alpha-carbon of the VLCFA moiety of the ceramide substrate to generate inositol phosphoceramide, one of three major sphingolipids in yeast |
742884 |
| 1.14.18.6 | physiological function |
FA2H knockdown in adipocytes increases diffusional mobility of raft-associated lipids, leading to reduced GLUT4 protein level, glucose uptake, and lipogenesis |
734433 |
| 1.14.18.6 | physiological function |
FA2H-siRNA suppresses 2-hydroxylase activity and decreases 2-hydroxyceramide/2-hydroxyglucosylceramide levels. Keratinocytes transduced with FA2H-siRNA contain abnormal epidermal lamellar bodies and do not form the normal extracellular lamellar membranes required for the epidermal permeability barrier |
734156 |
| 1.14.18.6 | physiological function |
fatty acid 2-hydroxylase Fa2h/UDP-galactose:ceramide galactosyltransferase Cgt double-deficient mice lack sulfatide, GalCer, and in addition 2-hydroxylated fatty acid-galactosylceramide and sphingomyelin. Compared to Cgt-/- mice the amount of GlcCer in central nervous system myelin is strongly reduced in Fa2h-/-/Cgt-/- mice by more than 80%. This is accompanied by a significant increase in sphingomyelin, which is the predominant sphingolipid in Fa2h-/-/Cgt-/- mice. Compact myelin is formed in Fa2h-/-/Cgt-/- mice, and g-ratios of myelinated axons in the spinal cord of 4-week-old Fa2h-/-/Cgt-/- mice do not differ significantly from that of Cgt-/- mice, and there is no obvious phenotypic difference between Fa2h-/-/Cgt-/- and Cgt-/- mice |
733584 |
