EC number:1.2.1.84
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.2 Acting on the aldehyde or oxo group of donors |
| 1.2.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.2.1.84 |
|---|---|
| Description: | Alcohol-forming fatty acyl-CoA reductase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.2.1.84 |
| BRENDA Enzyme Link: | BRENDA 1.2.1.84 |
| KEGG Enzyme Link: | KEGG1.2.1.84 |
| BioCyc Enzyme Link: | BioCyc 1.2.1.84 |
| ExPASy Enzyme Link: | ExPASy1.2.1.84 |
| EC2PDB Enzyme Link: | EC2PDB 1.2.1.84 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.2.1.84 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.2.1.84 |
| IntEnz Enzyme Link: | IntEnz 1.2.1.84 |
| MEDLINE Enzyme Link: | MEDLINE 1.2.1.84 |
| RHEA:52716 | a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[S;H0;+0:4]-[*:5].[*:6]-[C;H0;+0:7]1=[CH;+0:8]-[N;H0;+0:9](-[*:10])-[CH;+0:11]=[CH;+0:12]-[CH2;+0:13]-1.[*:14]-[C;H0;+0:15]1=[CH;+0:16]-[N;H0;+0:17](-[*:18])-[CH;+0:19]=[CH;+0:20]-[CH2;+0:21]-1.[H+;H0:22].[H+;H0:23]>>[*:1]-[CH2;+0:2]-[OH;+0:3].[*:5]-[SH;+0:4].[*:6]-[c;H0;+0:7]1:[cH;+0:8]:[n+;H0:9](-[*:10]):[cH;+0:11]:[cH;+0:12]:[cH;+0:13]:1.[*:14]-[c;H0;+0:15]1:[cH;+0:16]:[n+;H0:17](-[*:18]):[cH;+0:19]:[cH;+0:20]:[cH;+0:21]:1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Identification of amino acids conferring chain length substrate specificities on fatty alcohol-forming reductases FAR5 and FAR8 from Arabidopsis thaliana. | Chacón MG, Fournier AE, Tran F, Dittrich-Domergue F, Pulsifer IP, Domergue F, Rowland O | 2013 Oct 18 | 24005667 |
| Three Arabidopsis fatty acyl-coenzyme A reductases, FAR1, FAR4, and FAR5, generate primary fatty alcohols associated with suberin deposition. | Domergue F, Vishwanath SJ, Joubès J, Ono J, Lee JA, Bourdon M, Alhattab R, Lowe C, Pascal S, Lessire R, Rowland O | 2010 Aug | 20571114 |
| Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli. | Doan TT, Carlsson AS, Hamberg M, Bülow L, Stymne S, Olsson P | 2009 May 15 | 19062129 |
| Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed. | Metz JG, Pollard MR, Anderson L, Hayes TR, Lassner MW | 2000 Mar | 10712526 |
| CER4 encodes an alcohol-forming fatty acyl-coenzyme A reductase involved in cuticular wax production in Arabidopsis. | Rowland O, Zheng H, Hepworth SR, Lam P, Jetter R, Kunst L | 2006 Nov | 16980563 |
| Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. | Cheng JB, Russell DW | 2004 Sep 3 | 15220348 |
| RHEA:36319 | 2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) + octadecan-1-ol |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[C;H0;+0:10]1=[CH;+0:11]-[N;H0;+0:12](-[*:13])-[CH;+0:14]=[CH;+0:15]-[CH2;+0:16]-1.[*:17]-[S;H0;+0:18]-[C;H0;+0:19](-[*:20])=[O;H0;+0:21].[H+;H0:22].[H+;H0:23]>>[*:20]-[CH2;+0:19]-[OH;+0:21].[*:17]-[SH;+0:18].[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]-[c;H0;+0:10]1:[cH;+0:11]:[n+;H0:12](-[*:13]):[cH;+0:14]:[cH;+0:15]:[cH;+0:16]:1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. | Cheng JB, Russell DW | 2004 Sep 3 | 15220348 |
| RHEA:36315 | 2 H(+) + hexadecanoyl-CoA + 2 NADPH = 1-hexadecanol + CoA + 2 NADP(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[C;H0;+0:10]1=[CH;+0:11]-[N;H0;+0:12](-[*:13])-[CH;+0:14]=[CH;+0:15]-[CH2;+0:16]-1.[*:17]-[S;H0;+0:18]-[C;H0;+0:19](-[*:20])=[O;H0;+0:21].[H+;H0:22].[H+;H0:23]>>[*:20]-[CH2;+0:19]-[OH;+0:21].[*:17]-[SH;+0:18].[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]-[c;H0;+0:10]1:[cH;+0:11]:[n+;H0:12](-[*:13]):[cH;+0:14]:[cH;+0:15]:[cH;+0:16]:1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Biochemical characteristics of AtFAR2, a fatty acid reductase from Arabidopsis thaliana that reduces fatty acyl-CoA and -ACP substrates into fatty alcohols. | Doan TT, Carlsson AS, Stymne S, Hofvander P | 2016 | 27274541 |
| Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls ether glycerophospholipid synthesis. | Honsho M, Asaoku S, Fujiki Y | 2010 Mar 19 | 20071337 |
| Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. | Cheng JB, Russell DW | 2004 Sep 3 | 15220348 |