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Literature summary extracted from
- Structure of the pyrroloquinoline quinone radical in quinoprotein ethanol dehydrogenase (2006), J. Biol. Chem., 281, 1470-1476.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.1.2.8 | C105A/C106A | mutation of residues forming a characteristic disulfide ring in the binding pocket of pyrroloquinoline quinone. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone | Pseudomonas aeruginosa |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.2.8 | Pseudomonas aeruginosa | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.2.8 | ethanol + oxidized 2,6-dichlorophenolindophenol | - |
Pseudomonas aeruginosa | ethanal + reduced 2,6-dichlorophenolindophenol | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.5.5 | quinoprotein ethanol dehydrogenase | - |
- |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.2.8 | pyrroloquinoline quinone | the binding pocket of pyrroloquinoline quinone contains a characteristic disulphide ring formed by two adjacent cysteine residues. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone | Pseudomonas aeruginosa | |
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Release 2023.1 (January 2023)
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