1.1.5.2: glucose 1-dehydrogenase (PQQ, quinone) This is an abbreviated version! For detailed information about glucose 1-dehydrogenase (PQQ, quinone), go to the full flat file .
Reaction
D-glucose +
ubiquinone =
D-glucono-1,5-lactone +
ubiquinol
Synonyms (PQQ)GDH, aldose sugar dehydrogenase, Asd, beta-D-glucose:(acceptor) 1-oxidoreductase, D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase, dehydrogenase, glucose (pyrroloquinoline-quinone), EC 1.1.99.17, GCD, GDH, GDH-B, GDH1, GdhA, GDHm, GlcDH, glucose dehydrogenase, glucose dehydrogenase (PQQ dependent), glucose dehydrogenase (pyrroloquinoline-quinone), glucose dehydrogenase Amano 5, m-GDH, membrane glucose dehydrogenase, membrane-bound glucose dehydrogenase, membrane-bound PQQ-dependent glucose dehydrogenase, mGDH, PQQ GDH, PQQ glucose dehydrogenase, PQQ-dependent GDH, PQQ-dependent glucose dehydrogenase, PQQ-dependent mGDH, PQQ-dependent soluble glucose dehydrogenase, PQQ-GDH, PQQ-glucose dehydrogenase, PQQ-linked GCD, PQQ-sGDH, PqqC, PQQGDH, PQQGDH-B, pyrroloquinoline quinone dependent glucose dehydrogenase, pyrroloquinoline quinone glucose dehydrogenase, pyrroloquinoline quinone-dependent glucose dehydrogenase, QGDH, quinone-dependent glucose dehydrogenase, quinoprotein aldose sugar dehydrogenase, quinoprotein D-glucose dehydrogenase, quinoprotein glucose dehydrogenase, quinoprotein glucose DH, s-GDH, sGDH, sGDH-PQQ, soluble glucose dehydrogenase, soluble PQQ-dependent glucose dehydrogenase, soluble quinoprotein (PQQ-containing) glucose dehydrogenase, Tt_ASD, water-soluble PQQ glucose dehydrogenase, water-soluble pyrroquinoline quinone glucose dehydrogenase
ECTree
Cofactor
Cofactor on EC 1.1.5.2 - glucose 1-dehydrogenase (PQQ, quinone)
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additional information
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ruthenium(III) bispyridine compounds and ruthenium(III) 4-methyl-bispyridine compounds can act as artificial electron transfer mediator system
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
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prosthetic group
pyrroloquinoline quinone
prosthetic group
pyrroloquinoline quinone
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dependent on
pyrroloquinoline quinone
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coenzyme
pyrroloquinoline quinone
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required for activity
pyrroloquinoline quinone
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during the processing of pyrroloquinoline quinone into the apoenzyme to give active enzyme, its affinity is markedly dependent on the pH, four groups with pK values between pH 7 and pH 8 are involved
pyrroloquinoline quinone
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each subunit of the dimer contains one molecule of pyrroloquinoline quinone
pyrroloquinoline quinone
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reconstitution of the apoenzyme to full activity is achieved with a stoichiometric amount of pyrroloquinoline quinone. Mg2+ anchors pyrroloquinoline quinone cofactor to the enzyme protein and activates the bound cofactor
pyrroloquinoline quinone
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cofactor required
pyrroloquinoline quinone
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type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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Sinorhizobium meliloti is unable to synthesize pyrroloquinoline quinone, synthesis of the holoenzyme in alfalfa nodules
pyrroloquinoline quinone
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organisms with an active holoenzyme
pyrroloquinoline quinone
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organisms with an active holoenzyme
pyrroloquinoline quinone
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organisms with an active holoenzyme
pyrroloquinoline quinone
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organisms with an active holoenzyme
pyrroloquinoline quinone
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organisms with an inactive apoenzyme
pyrroloquinoline quinone
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organisms with an inactive apoenzyme
pyrroloquinoline quinone
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the apoenzyme is converted to the holoenzyme with exogenous pyrroloquinoline quinone and Mg2+. The holoenzyme gradually returns to the apoenzyme in absence of pyrroloquinoline quinone and/or Mg2+
pyrroloquinoline quinone
i.e. PQQ
pyrroloquinoline quinone
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i.e. PQQ, dependent on
pyrroloquinoline quinone
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i.e. PQQ, dependent on
pyrroloquinoline quinone
i.e. PQQ, dependent on
pyrroloquinoline quinone
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i.e. PQQ, dependent on exogenous PQQ, since Escherichia coli does not synthesize PQQ itself
pyrroloquinoline quinone
i.e. PQQ, dependent on, Escherichia coli needs to be reconstituted with PQQ for activity
pyrroloquinoline quinone
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i.e. PQQ, dependent on, functions as a redox mediator by transfer of hydride ions and electrons, redox-related structural changes, overview
pyrroloquinoline quinone
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i.e. PQQ, or 2,7,9-tricarboxy-1H-pyrrolo [2,3-f]-quinoline-4,5-dione, residues Gln231, Gln246, Ala350, and Leu376 are involved in binding
pyrroloquinoline quinone
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PQQ
pyrroloquinoline quinone
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PQQ
pyrroloquinoline quinone
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PQQ
pyrroloquinoline quinone
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contains one pyrroloquinoline quinone per subunit
pyrroloquinoline quinone
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contains one pyrroloquinoline quinone per subunit, pyrroloquinoline quinone (PQQ) is 2,7,9 tricarboxy-1H-pyrrolo [2,3-f]-quinoline-4,5-dione
pyrroloquinoline quinone
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i.e. 2,7,9,-tricarboxyl-1H-pyrrolo[2,3-f]quinoline-4,5-dione
pyrroloquinoline quinone
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apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
pyrroloquinoline quinone
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i.e. 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid, prosthetic group, not covalently linked to the polypeptide chain or posttranslationally derived from precursor amino acid residues in the active site of the constituent. enzyme. Biosynthesis of the cofactor in Klebsiella pneumoniae is facilitated by six genes, pqqABCDEF. PqqC is one of two metal free oxidases of known structure and catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid, overview
pyrroloquinoline quinone
PQQ, essential cofactor for enzyme activity, essential role of pqqABCDEF in PQQ biosynthesis, overview
pyrroloquinoline quinone
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quinoprotein, required for QGDH activity
pyrroloquinoline quinone
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required for catalysis, one molecule per enzyme subunit