| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.3.1.93 |
|---|---|
| Description: | Very-long-chain enoyl-CoA reductase. |
| Cath: | 3.10.20.90; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.3.1.93 |
| BRENDA Enzyme Link: | BRENDA 1.3.1.93 |
| KEGG Enzyme Link: | KEGG1.3.1.93 |
| BioCyc Enzyme Link: | BioCyc 1.3.1.93 |
| ExPASy Enzyme Link: | ExPASy1.3.1.93 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.1.93 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.1.93 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.1.93 |
| IntEnz Enzyme Link: | IntEnz 1.3.1.93 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.1.93 |
| RHEA:14473 | a very-long-chain 2,3-saturated fatty acyl-CoA + NADP(+) = a very-long-chain (2E)-enoyl-CoA + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[*:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[C;H0;+0:6]1=[CH;+0:12]-[N;H0;+0:10](-[*:11])-[CH;+0:9]=[CH;+0:8]-[CH2;+0:7]-1.[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. | Kvam E, Gable K, Dunn TM, Goldfarb DS | 2005 Sep | 15958487 |
| Disruptions of the Arabidopsis Enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis. | Zheng H, Rowland O, Kunst L | 2005 May | 15829606 |
| Functional characterization of the Arabidopsis thaliana orthologue of Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating system. | Gable K, Garton S, Napier JA, Dunn TM | 2004 Feb | 14673020 |
| Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. | Kohlwein SD, Eder S, Oh CS, Martin CE, Gable K, Bacikova D, Dunn T | 2001 Jan | 11113186 |