EC number:1.1.1.n12
| ID: | 1.1.1.n12 |
|---|---|
| Description: | (3R)-hydroxyacyl-CoA dehydrogenase. |
| Cath: | 3.30.1050.10; 3.30.160.260; 3.40.50.720; 3.10.129.10; |
3D structure
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| RHEA:32711 | a (3R)-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[C;H0;+0:6]1=[CH;+0:12]-[N;H0;+0:10](-[*:11])-[CH;+0:9]=[CH;+0:8]-[CH2;+0:7]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. | Jiang LL, Miyazawa S, Souri M, Hashimoto T | 1997 Feb | 9089413 |
| Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins. | Dieuaide-Noubhani M, Novikov D, Baumgart E, Vanhooren JC, Fransen M, Goethals M, Vandekerckhove J, Van Veldhoven PP, Mannaerts GP | 1996 Sep 15 | 8856068 |
| Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics. | Haataja TJ, Koski MK, Hiltunen JK, Glumoff T | 2011 May 1 | 21320074 |