EC number:1.3.1.74
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: | 1.3.1.74 |
|---|---|
| Description: | 2-alkenal reductase (NAD(P)(+)). |
| Alternative Name: |
NADPH:2-alkenal alpha,beta-hydrogenase. NAD(P)H-dependent alkenal/one oxidoreductase. 2-alkenal reductase. |
| Cath: | 1.10.286.90; 1.20.1250.20; 3.40.50.720; 3.40.830.10; 3.90.180.10; 3.90.70.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.3.1.74 |
| BRENDA Enzyme Link: | BRENDA 1.3.1.74 |
| KEGG Enzyme Link: | KEGG1.3.1.74 |
| BioCyc Enzyme Link: | BioCyc 1.3.1.74 |
| ExPASy Enzyme Link: | ExPASy1.3.1.74 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.1.74 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.1.74 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.1.74 |
| IntEnz Enzyme Link: | IntEnz 1.3.1.74 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.1.74 |
| RHEA:13737 | an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH |
| 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 |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Protection against photooxidative injury of tobacco leaves by 2-alkenal reductase. Detoxication of lipid peroxide-derived reactive carbonyls. | Mano J, Belles-Boix E, Babiychuk E, Inzé D, Torii Y, Hiraoka E, Takimoto K, Slooten L, Asada K, Kushnir S | 2005 Dec | 16299173 |
| The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis catalyzes the alpha,beta-hydrogenation of 2-alkenals: detoxication of the lipid peroxide-derived reactive aldehydes. | Mano J, Torii Y, Hayashi S, Takimoto K, Matsui K, Nakamura K, Inzé D, Babiychuk E, Kushnir S, Asada K | 2002 Dec | 12514241 |
| Antioxidative function and substrate specificity of NAD(P)H-dependent alkenal/one oxidoreductase. A new role for leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin 13-reductase. | Dick RA, Kwak MK, Sutter TR, Kensler TW | 2001 Nov 2 | 11524419 |
| RHEA:13733 | an n-alkanal + NAD(+) = an alk-2-enal + 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 |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Protection against photooxidative injury of tobacco leaves by 2-alkenal reductase. Detoxication of lipid peroxide-derived reactive carbonyls. | Mano J, Belles-Boix E, Babiychuk E, Inzé D, Torii Y, Hiraoka E, Takimoto K, Slooten L, Asada K, Kushnir S | 2005 Dec | 16299173 |
| The NADPH:quinone oxidoreductase P1-zeta-crystallin in Arabidopsis catalyzes the alpha,beta-hydrogenation of 2-alkenals: detoxication of the lipid peroxide-derived reactive aldehydes. | Mano J, Torii Y, Hayashi S, Takimoto K, Matsui K, Nakamura K, Inzé D, Babiychuk E, Kushnir S, Asada K | 2002 Dec | 12514241 |
| Antioxidative function and substrate specificity of NAD(P)H-dependent alkenal/one oxidoreductase. A new role for leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin 13-reductase. | Dick RA, Kwak MK, Sutter TR, Kensler TW | 2001 Nov 2 | 11524419 |