ENZYME entry: EC 1.1.5.2
Accepted Name |
quinoprotein glucose dehydrogenase (PQQ, quinone).
|
Alternative Name(s) |
D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase. |
glucose dehydrogenase (PQQ-dependent). |
glucose dehydrogenase (pyrroloquinoline-quinone). |
quinoprotein D-glucose dehydrogenase. |
Reaction catalysed |
a ubiquinone + D-glucose <=> a ubiquinol + D-glucono-1,5-lactone |
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 |
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 |
Rhea expert-curated reactions | 1.1.5.2 |
UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.1.5.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-