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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.

Word Map on EC 1.1.5.2

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

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.5 With a quinone or similar compound as acceptor
                1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone)

Temperature Stability

Temperature Stability on EC 1.1.5.2 - glucose 1-dehydrogenase (PQQ, quinone)

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
the enzyme is extremely thermostable, and the activity of the pyrroloquinoline quinone-bound holoenzyme is not lost after incubation at 100 °C for 10 min, while the apoenzyme retains full activity at up to 80°C under the same conditions
25 - 65
-
100% activity at 25-30°C, about 90% activity at 35°C, about 80% activity at 40-45°C, about 750% activity at 50°C, about 60% activity at 55°C, after incubation at 60°C for 1 h the enzyme still has 27% of its initial activity while loosing nearly all activity after treatment at 65°C
35
-
pH 6, 10 min, in absence of Ca2+, stable below, reversible inactivation above
40
-
no activity after 10 min at 40°C
40 - 50
-
low temperature of below 40°C has the stable and highest enzyme activity after kept for 120 min. Increase of storage temperature to over 50°C inhibits the activity of above 58% after 10 min treatment, while no activity is detected after incubation for 60 min at 60 or 70°C
40.5
10 min, 50% inactivation of recombinant mutant D354N apoenzyme
40.8
10 min, 50% inactivation of recombinant wild-type apoenzyme
41
10 min, 50% inactivation of recombinant mutant D354N/N355D apoenzyme
43.2
10 min, 50% inactivation of recombinant mutant N355D apoenzyme
45
-
20 min, 20% loss of activity of native enzyme, about 50% loss of activity of linked-dimeric enzyme
46
-
half-life temperature of the holoenzyme
48
-
activity decreases at 48°C and above
48.6
10 min, 50% inactivation of recombinant mutant D354N/N355D holoenzyme
49
10 min, 50% inactivation of recombinant mutant D354N holoenzyme
50
-
pH 6, 10 min, in presence of Ca2+, inactivation above
51
10 min, 50% inactivation of recombinant wild-type holoenzyme
70
-
10 min, mutant S145C retaines 90% of wild-type activity
85
half-life of apoenzyme: about 25 min. Activity of the pyrroloquinoline quinone-bound holoenzyme is not lost after incubation at 85°C for 100 min
additional information
-
the C-terminal 3% region, A3 region, plays an important role in the increase of thermal stability