EC number:1.14.18.6
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.18.6 |
|---|---|
| Description: | 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.18.6 |
| BRENDA Enzyme Link: | BRENDA 1.14.18.6 |
| KEGG Enzyme Link: | KEGG1.14.18.6 |
| BioCyc Enzyme Link: | BioCyc 1.14.18.6 |
| ExPASy Enzyme Link: | ExPASy1.14.18.6 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.18.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.18.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.18.6 |
| IntEnz Enzyme Link: | IntEnz 1.14.18.6 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.18.6 |
EC number:1.14.18.6
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:46520 | 2 [Fe(II)-cytochrome b5] + a N-[1,2 saturated-(4R)-hydroxyacyl]sphinganine + 2 H(+) + O2 = 2 [Fe(III)-cytochrome b5] + a N-[(2'R)-(4R)-hydroxyacyl]sphinganine + H2O |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[Fe+2;H0:4].[Fe+2;H0:5].[H+;H0:6].[H+;H0:7].[O;H0;+0:8]=[O;H0;+0:9]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:8].[Fe+3;H0:4].[Fe+3;H0:5].[OH2;+0:9] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. | Mitchell AG, Martin CE | 1997 Nov 7 | 9353282 |
| Stereospecificity of fatty acid 2-hydroxylase and differential functions of 2-hydroxy fatty acid enantiomers. | Guo L, Zhang X, Zhou D, Okunade AL, Su X | 2012 Jul | 22517924 |
| The human FA2H gene encodes a fatty acid 2-hydroxylase. | Alderson NL, Rembiesa BM, Walla MD, Bielawska A, Bielawski J, Hama H | 2004 Nov 19 | 15337768 |
| Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain. | Dunn TM, Haak D, Monaghan E, Beeler TJ | 1998 Mar 15 | 9559540 |
| A mammalian fatty acid hydroxylase responsible for the formation of alpha-hydroxylated galactosylceramide in myelin. | Eckhardt M, Yaghootfam A, Fewou SN, Zöller I, Gieselmann V | 2005 May 15 | 15658937 |