EC number:1.1.98.4
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.98 With other, known, physiological acceptors |
| ID: | 1.1.98.4 |
|---|---|
| Description: | F420H(2):quinone oxidoreductase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.98.4 |
| BRENDA Enzyme Link: | BRENDA 1.1.98.4 |
| KEGG Enzyme Link: | KEGG1.1.98.4 |
| BioCyc Enzyme Link: | BioCyc 1.1.98.4 |
| ExPASy Enzyme Link: | ExPASy1.1.98.4 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.98.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.98.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.98.4 |
| IntEnz Enzyme Link: | IntEnz 1.1.98.4 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.98.4 |
| RHEA:39663 | a quinol + H(+) + oxidized coenzyme F420-(gamma-Glu)(n) = a quinone + reduced coenzyme F420-(gamma-Glu)(n) |
| RULE(radius=1) | [*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[OH;+0:4]):[c;H0;+0:5](-[*:6]):[c;H0;+0:7](-[*:8]):[c;H0;+0:9](-[OH;+0:10]):[c;H0;+0:11]:1-[*:12].[*:13]-[n;H0;+0:14]1:[*:15]:[*:16]:[cH;+0:17]:[c;H0;+0:18](:[*:19])-[c;H0;+0:20]:1:[n;H0;+0:21]:[*:22].[H+;H0:23]>>[*:1]-[C;H0;+0:2]1=[C;H0;+0:11](-[*:12])-[C;H0;+0:9](=[O;H0;+0:10])-[C;H0;+0:7](-[*:8])=[C;H0;+0:5](-[*:6])-[C;H0;+0:3]-1=[O;H0;+0:4].[*:13]-[N;H0;+0:14]1-[*:15]:[*:16]-[CH2;+0:17]-[c;H0;+0:18](:[*:19]):[c;H0;+0:20]-1:[nH;+0:21]:[*:22] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| F420H2: quinone oxidoreductase from Archaeoglobus fulgidus. Characterization of a membrane-bound multisubunit complex containing FAD and iron-sulfur clusters. | Kunow J, Linder D, Stetter KO, Thauer RK | 1994 Jul 15 | 8055920 |
| Structure of the F420H2:quinone oxidoreductase of Archaeoglobus fulgidus identification and overproduction of the F420H2-oxidizing subunit. | Brüggemann H, Falinski F, Deppenmeier U | 2000 Sep | 10971593 |