EC Number   |
Cofactor |
Reference |
|---|
   1.1.2.7 | pyrroloquinoline quinone |
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview |
684666 |
| 1.1.2.7 | pyrroloquinoline quinone |
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure |
690794 |
| 1.1.2.7 | pyrroloquinoline quinone |
PQQ, prosthetic group |
684950 |
| 1.1.2.7 | pyrroloquinoline quinone |
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview |
685050 |
| 1.1.2.7 | pyrroloquinoline quinone |
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview |
689815 |
| 1.1.2.7 | pyrroloquinoline quinone |
prosthetic group, 1.3 molecules per enzyme molecule |
687432 |
| 1.1.2.7 | pyrroloquinoline quinone |
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview |
724176 |
| 1.1.2.7 | pyrroloquinoline quinone |
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview |
671068 |
| 1.1.2.7 | pyrroloquinoline quinone |
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule |
687486 |
