EC number:7.1.1.5
Enzyme
Download| EC Tree |
| 7. Translocases |
| 7.1 Catalysing the translocation of hydrons |
| 7.1.1 Linked to oxidoreductase reactions |
| ID: | 7.1.1.5 |
|---|---|
| Description: | Menaquinol oxidase (H(+)-transporting). |
| Alternative Name: |
Cytochrome bd oxidase. Cytochrome aa3-600 oxidase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 7.1.1.5 |
| BRENDA Enzyme Link: | BRENDA 7.1.1.5 |
| KEGG Enzyme Link: | KEGG7.1.1.5 |
| BioCyc Enzyme Link: | BioCyc 7.1.1.5 |
| ExPASy Enzyme Link: | ExPASy7.1.1.5 |
| EC2PDB Enzyme Link: | EC2PDB 7.1.1.5 |
| ExplorEnz Enzyme Link: | ExplorEnz 7.1.1.5 |
| PRIAM enzyme-specific profiles Link: | PRIAM 7.1.1.5 |
| IntEnz Enzyme Link: | IntEnz 7.1.1.5 |
| MEDLINE Enzyme Link: | MEDLINE 7.1.1.5 |
| RHEA:30259 | 2 a menaquinol + O2 = 2 a menaquinone + 2 H2O |
| RULE(radius=1) | [*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5](-[OH;+0:6]):[*:7]:[*:8]:[c;H0;+0:9]:1-[OH;+0:10].[*:11]-[c;H0;+0:12]1:[c;H0;+0:13](-[OH;+0:14]):[*:15]:[*:16]:[c;H0;+0:17](-[OH;+0:18]):[c;H0;+0:19]:1-[*:20].[O;H0;+0:21]=[O;H0;+0:22]>>[*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[*:7]:[*:8]-[C;H0;+0:9]-1=[O;H0;+0:10].[*:11]-[C;H0;+0:12]1=[C;H0;+0:19](-[*:20])-[C;H0;+0:17](=[O;H0;+0:18])-[*:16]:[*:15]-[C;H0;+0:13]-1=[O;H0;+0:14].[OH2;+0:21].[OH2;+0:22] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The terminal quinol oxidases of Bacillus subtilis have different energy conservation properties. | Lauraeus M, Wikström M | 1993 May 25 | 8388393 |
| Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis. | Lemma E, Simon J, Schägger H, Kröger A | 1995 Jun | 7575098 |
| Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis. | Yi SM, Narasimhulu KV, Samoilova RI, Gennis RB, Dikanov SA | 2010 Jun 11 | 20351111 |