EC number:1.23.5.1
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.23 Reducing C-O-C group as acceptor |
| 1.23.5 With a quinone or similar compound as acceptor |
| ID: | 1.23.5.1 |
|---|---|
| Description: | Violaxanthin de-epoxidase. |
| Alternative Name: |
VDE. |
| Cath: | 2.40.128.20; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.23.5.1 |
| BRENDA Enzyme Link: | BRENDA 1.23.5.1 |
| KEGG Enzyme Link: | KEGG1.23.5.1 |
| BioCyc Enzyme Link: | BioCyc 1.23.5.1 |
| ExPASy Enzyme Link: | ExPASy1.23.5.1 |
| EC2PDB Enzyme Link: | EC2PDB 1.23.5.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.23.5.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.23.5.1 |
| IntEnz Enzyme Link: | IntEnz 1.23.5.1 |
| MEDLINE Enzyme Link: | MEDLINE 1.23.5.1 |
| RHEA:32371 | all-trans-violaxanthin + 2 L-ascorbate = all-trans-zeaxanthin + 2 H2O + 2 L-dehydroascorbate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[OH;+0:3])=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]-[C;H0;+0:8](-[OH;+0:9])=[C;H0;+0:10](-[*:11])-[OH;+0:12].([*:13]-[C;H0;+0:14]1(-[*:15])-[O;H0;+0:16]-[C;H0;+0:17]-1(-[*:18])-[*:19].[*:20]-[C;H0;+0:21]1(-[*:22])-[O;H0;+0:23]-[C;H0;+0:24]-1(-[*:25])-[*:26])>>([*:13]-[C;H0;+0:14](-[*:15])=[C;H0;+0:17](-[*:18])-[*:19].[*:20]-[C;H0;+0:21](-[*:22])=[C;H0;+0:24](-[*:25])-[*:26]).[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[C;H0;+0:4](-[*:5])=[O;H0;+0:6].[*:7]-[C;H0;+0:8](=[O;H0;+0:9])-[C;H0;+0:10](-[*:11])=[O;H0;+0:12].[OH2;+0:23].[OH2;+0:16] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. | Bugos RC, Hieber AD, Yamamoto HY | 1998 Jun 19 | 9624110 |
| Violaxanthin de-epoxidase. | Rockholm DC, Yamamoto HY | 1996 Feb | 8742341 |
| Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity. | Latowski D, Akerlund HE, Strzałka K | 2004 Apr 20 | 15078086 |
| Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae). | Goss R | 2003 Sep | 12748855 |
| Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers. | Latowski D, Kruk J, Burda K, Skrzynecka-Jaskier M, Kostecka-Gugała A, Strzałka K | 2002 Sep | 12230579 |
| Characterization of violaxanthin de-epoxidase purified in the presence of Tween 20: effects of dithiothreitol and pepstatin A. | Kuwabara T, Hasegawa M, Kawano M, Takaichi S | 1999 Nov | 10635115 |
| Violaxanthin de-epoxidase. Lipid composition and substrate specificity. | Yamamoto HY, Higashi RM | 1978 Oct | 102251 |