Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 | Klebsiella pneumoniae | - |
4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella pneumoniae | P27505 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 | - |
Klebsiella pneumoniae | 4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylate + 2 H2O2 + 2 H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PqqC | - |
Klebsiella pneumoniae |
quinoprotein dehydrogenase | - |
Klebsiella pneumoniae |
General Information | Comment | Organism |
---|---|---|
additional information | an all atom model of the quinoprotein dehydrogenase PqqC in complex with 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid (PQQ) and O2, solvated with TIP3 water in periodic boxes, is subjected to random-acceleration molecular dynamics (RAMD) showing that O2 leaves the active binding pocket, in front of PQQ, to get to the solvent, as easily as with a variety of other O2-activating enzymes, O2 carriers, and gas-sensing proteins. The shortest pathway, orthogonal to the center of the mean plane of PQQ, is largely preferred by O2 over pathways slightly deviating from this line. These observations challenge the interpretation of an impermeable active binding pocket of PqqC-PQQ, as drawn from both X-ray diffraction data of the crystal at low temperature and physiological experimentation. Key residues for the minor O2 gates are 1. Q155, L158, R177, and R17, 2. E188, and L191, and 3. D83 and Q182, or the main O2 egress involving residues P151, L180, and A183, modeling, overview | Klebsiella pneumoniae |