EC number:1.3.3.11
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.3 With oxygen as acceptor |
| ID: | 1.3.3.11 |
|---|---|
| Description: | Pyrroloquinoline-quinone synthase. |
| Cath: | 1.10.1240.20; 1.20.910.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.3.3.11 |
| BRENDA Enzyme Link: | BRENDA 1.3.3.11 |
| KEGG Enzyme Link: | KEGG1.3.3.11 |
| BioCyc Enzyme Link: | BioCyc 1.3.3.11 |
| ExPASy Enzyme Link: | ExPASy1.3.3.11 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.3.11 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.3.11 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.3.11 |
| IntEnz Enzyme Link: | IntEnz 1.3.3.11 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.3.11 |
| RHEA:10692 | 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = H(+) + 2 H2O + 2 H2O2 + pyrroloquinoline quinone |
| RULE(radius=1) | [*:1]-[CH;+0:2]1-[CH2;+0:3]-[CH;+0:4](-[*:5])-[C;H0;+0:6]2=[C;H0;+0:7](-[*:8]-[*:9]-[C;H0;+0:10](-[CH2;+0:11]-[CH;+0:12](-[*:13])-[NH2;+0:14])=[CH;+0:15]-2)-[NH;+0:16]-1.[O;H0;+0:17]=[O;H0;+0:18].[O;H0;+0:19]=[O;H0;+0:20].[O;H0;+0:21]=[O;H0;+0:22]>>[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[c;H0;+0:6]2:[c;H0;+0:7](:[n;H0;+0:16]:1)-[*:8]-[*:9]-[c;H0;+0:10]1:[cH;+0:11]:[c;H0;+0:12](-[*:13]):[nH;+0:14]:[c;H0;+0:15]:1-2.[OH2;+0:21].[OH2;+0:22].[OH;+0:17]-[OH;+0:18].[OH;+0:19]-[OH;+0:20] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone. | Magnusson OT, Toyama H, Saeki M, Rojas A, Reed JC, Liddington RC, Klinman JP, Schwarzenbacher R | 2004 May 25 | 15148379 |
| The structure of a biosynthetic intermediate of pyrroloquinoline quinone (PQQ) and elucidation of the final step of PQQ biosynthesis. | Magnusson OT, Toyama H, Saeki M, Schwarzenbacher R, Klinman JP | 2004 May 5 | 15113189 |