1.1.1.47: glucose 1-dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about glucose 1-dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.47
Reaction
Synonyms
alkali-resistant glucose 1-dehydrogenase, beta-D-glucose:NAD(P)+ 1-oxido-reductase, beta-D-glucose:NAD(P)+ 1-oxidoreductase, BmGlcDH-III, BmGlcDH-IV, bzgdh, D-glucose dehydrogenase (NAD(P)), EC 1.1.5.2, GDH, gdh-2, GDHB, general stress protein 74, GlcDH, GlcDH-I, GlcDH-II, GlcDH-IWG3, glucose 1-dehydrogenase, glucose 1-dehydrogenase 3, glucose 1-dehydrogenase B, glucose 1-dehydrogenase III, glucose 1-dehydrogenase IV, glucose dehydrogenase, glucose1-dehydrogenase, GluDH, GSP74, hexose phosphate dehydrogenase, hexose-6-phosphate dehydrogenase, LsGDH, More, NAD(P)-dependent glucose 1-dehydrogenase, NAD(P)-dependent glucose dehydrogenase, NAD(P)-dependent glucose-1-dehydrogenase, NAD-GDH, nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase, SsGDH, SSO3204
ECTree
1.1.1.47 glucose 1-dehydrogenase [NAD(P)+]Advanced search results
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results (pH Stability
pH Stability on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]
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pH STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3 - 11
-
after 30 min at pH 3.0-11.0, the enzyme maintains activity of more than 70%
740857
4 - 10
-
30°C, 20 min, mutant enzymes E96K and E95A, less than 20% loss of activity
639105
4 - 10.5
-
the enzyme is extremely stable over a broad pH ranges from 4.0 to 10.5 and retains more than 80% of its original activity after incubation at pH values ranging from 4.5 to 10.5
740382
4 - 8.5
1 h incubation, the enzyme maintains around 80% of its initial activity
763151
5
-
30°C, 20 min, about 55% loss of activity of mutant enzyme Y253C, about 35% loss of activity of mutant enzyme E96G and wild-type enzyme
639105
6.5 - 10.5
most stable at pH 8.5, retains more than 80% activity at pH 6.5-10.5 after 1 h at 25°C, more than 30% activity after 24 h at pH 10.0
711501
6.5 - 7
-
20 min, without NaCl, isoenzyme GlcDH-IWG3 and GlcDH-III are stable
639101
6.5 - 9
-
the enzyme is stable and active at pH 6.5, by shifting the pH to 9.0 the enzyme is completely and irreversibly dissociated into four inactive protomers
639108
7 - 9
wild type GlcDH shows reversible dissociation-association between inactive monomers and active tetramers when the pH is shifted between 9 and 7
677657
additional information
8
-
30°C, 20 min, about 50% loss of activity of mutant enzyme Y253C, about 80% loss of wild-type enzyme, about 30% loss of activity of mutant enzyme E96G and E96, about 15% loss of activity of mutant enzyme E96K
639105
9
-
the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9 the enzyme is completely and reversibly dissociated into four inactive protomers
639108, 639112
9
after dissociation of the tetrameric enzyme into its inactive monomers at pH 9 two tyrosine residues (Tyr-254 and Tyr-160) become susceptible to nitration which are unable to reassociate to the tetramer
679608
additional information
-
shifting the pH from 6.5 to 9.0 leads to inactivation, reactivation to 100% activity by shifting pH back to 6.5, protein concentration higher than 0.1 mg/ml
639103
additional information
-
isoenzyme GlcDHIII has no stable pH-region without NaCl
639101
