| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.3.1.9 |
|---|---|
| Description: | Enoyl-[acyl-carrier-protein] reductase (NADH). |
| Alternative Name: |
NADH-specific enoyl-ACP reductase. NADH-enoyl acyl carrier protein reductase. Enoyl-ACP reductase. |
| Cath: | 1.10.110.40; 1.10.287.3140; 1.10.8.40; 1.10.8.400; 1.20.1050.120; 1.20.5.3540; 3.20.20.70; 3.30.1120.10; 3.30.1120.100; 3.30.70.2420; |
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 1.3.1.9 |
| BRENDA Enzyme Link: | BRENDA 1.3.1.9 |
| KEGG Enzyme Link: | KEGG1.3.1.9 |
| BioCyc Enzyme Link: | BioCyc 1.3.1.9 |
| ExPASy Enzyme Link: | ExPASy1.3.1.9 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.1.9 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.1.9 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.1.9 |
| IntEnz Enzyme Link: | IntEnz 1.3.1.9 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.1.9 |
| RHEA:10240 | a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + H(+) + NADH |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acyl-carrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves. | Shimakata T, Stumpf PK | 1982 Oct 1 | 6756317 |
| Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli. | Weeks G, Wakil SJ | 1968 Mar 25 | 4384650 |
| In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli. | Yu X, Liu T, Zhu F, Khosla C | 2011 Nov 15 | 22042840 |