EC number:1.3.1.34
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.3.1.34 | ||
|---|---|---|---|
| Description: | 2,4-dienoyl-CoA reductase (NADPH). | ||
| Alternative Name: |
4-enoyl-CoA reductase (NADPH). | ||
| Prosite: | PDOC00060; | ||
| PDB: |
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| Cath: | 3.20.20.70; 3.40.50.720; 3.50.50.60; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.3.1.34 |
| BRENDA Enzyme Link: | BRENDA 1.3.1.34 |
| KEGG Enzyme Link: | KEGG1.3.1.34 |
| BioCyc Enzyme Link: | BioCyc 1.3.1.34 |
| ExPASy Enzyme Link: | ExPASy1.3.1.34 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.1.34 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.1.34 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.1.34 |
| IntEnz Enzyme Link: | IntEnz 1.3.1.34 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.1.34 |
| RHEA:12136 | 4,5-saturated-(2E)-enoyl-CoA + NADP(+) = (2E,4E)-dienoyl-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 |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli. | He XY, Yang SY, Schulz H | 1997 Sep 1 | 9346310 |
| Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria. | Kunau WH, Dommes P | 1978 Nov 15 | 729581 |
| Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. | Dommes V, Luster W, Cvetanović M, Kunau WH | 1982 Jul | 6749495 |
| 2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia coli. Comparison of properties. | Dommes V, Kunau WH | 1984 Feb 10 | 6363415 |
| Two distinct proton donors at the active site of Escherichia coli 2,4-dienoyl-CoA reductase are responsible for the formation of different products. | Tu X, Hubbard PA, Kim JJ, Schulz H | 2008 Jan 29 | 18171025 |
| Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase. | De Nys K, Meyhi E, Mannaerts GP, Fransen M, Van Veldhoven PP | 2001 Aug 29 | 11514237 |