EC number:1.1.5.5
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.5 With a quinone or similar compound as acceptor |
| ID: | 1.1.5.5 |
|---|---|
| Description: | Alcohol dehydrogenase (quinone). |
| Alternative Name: |
Type III ADH. Quinoprotein alcohol dehydrogenase. Quinoprotein ADH. Pyrroloquinoline quinone-dependent alcohol dehydrogenase. PQQ-dependent alcohol dehydrogenase. PQQ-dependent ADH. PQQ alcohol dehydrogenase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.5.5 |
| BRENDA Enzyme Link: | BRENDA 1.1.5.5 |
| KEGG Enzyme Link: | KEGG1.1.5.5 |
| BioCyc Enzyme Link: | BioCyc 1.1.5.5 |
| ExPASy Enzyme Link: | ExPASy1.1.5.5 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.5.5 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.5.5 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.5.5 |
| IntEnz Enzyme Link: | IntEnz 1.1.5.5 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.5.5 |
| RHEA:26442 | a ubiquinone + ethanol = a ubiquinol + acetaldehyde |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[*:13]-[CH2;+0:14]-[OH;+0:15]>>[*:13]-[CH;+0:14]=[O;H0;+0:15].[*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:7](-[*:8]):[c;H0;+0:9](-[*:10]):[c;H0;+0:11]:1-[OH;+0:12] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The quinohemoprotein alcohol dehydrogenase of Gluconobacter suboxydans has ubiquinol oxidation activity at a site different from the ubiquinone reduction site. | Matsushita K, Yakushi T, Toyama H, Adachi O, Miyoshi H, Tagami E, Sakamoto K | 1999 Jan 5 | 9878716 |
| Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans. | Matsushita K, Yakushi T, Toyama H, Shinagawa E, Adachi O | 1996 Mar 1 | 8617755 |
| Generation mechanism and purification of an inactive form convertible in vivo to the active form of quinoprotein alcohol dehydrogenase in Gluconobacter suboxydans. | Matsushita K, Yakushi T, Takaki Y, Toyama H, Adachi O | 1995 Nov | 7592433 |
| A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans. | Matsushita K, Kobayashi Y, Mizuguchi M, Toyama H, Adachi O, Sakamoto K, Miyoshi H | 2008 Oct | 18838797 |
| The PQQ-alcohol dehydrogenase of Gluconacetobacter diazotrophicus. | Gómez-Manzo S, Contreras-Zentella M, González-Valdez A, Sosa-Torres M, Arreguín-Espinoza R, Escamilla-Marván E | 2008 Jun 30 | 18321602 |
| [Goat smallpox in Chad: study of the pathogeny of the virus in sheep and goats]. | Bidjeh K, Ganda K, Diguimbaye C | 1991 | 1663645 |