ENZYME entry: EC 1.1.5.2
| Accepted Name |
| Quinoprotein glucose dehydrogenase.
|
| Alternative Name(s) |
| D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase. |
| Glucose dehydrogenase (PQQ-dependent). |
| Glucose dehydrogenase (pyrroloquinoline-quinone). |
| Quinoprotein D-glucose dehydrogenase. |
| Reaction catalysed |
| D-glucose + ubiquinone <=> D-glucono-1,5-lactone + ubiquinol |
| Cofactor(s) |
| Calcium or magnesium; Pyrroloquinoline quinone.
|
| Comment(s) |
- Integral membrane protein containing PQQ as prosthetic group.
- It also contains bound ubiquinone and Mg(2+) or Ca(2+).
- Electron acceptor is membrane ubiquinone but usually assayed with
phenazine methosulfate.
- Like in all other quinoprotein alcohol dehydrogenases the catalytic
domain has an 8-bladed 'propeller' structure.
- It occurs in a wide range of bacteria.
- Catalyzes a direct oxidation of the pyranose form of D-glucose to the
lactone and thence to D-gluconate in the periplasm.
- Oxidizes other monosaccharides including the pyranose forms of
pentoses.
- Formerly EC 1.1.99.17.
|
| Cross-references |
| PROSITE | PDOC00375 |
| BRENDA | 1.1.5.2 |
| EC2PDB | 1.1.5.2 |
| ExplorEnz | 1.1.5.2 |
| PRIAM enzyme-specific profiles | 1.1.5.2 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.1.5.2 |
| IUBMB Enzyme Nomenclature | 1.1.5.2 |
| IntEnz | 1.1.5.2 |
| MEDLINE | Find literature relating to 1.1.5.2 |
| MetaCyc | 1.1.5.2 |
| UniProtKB/Swiss-Prot |
|
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