Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

D-glucose
+
NAD(P)+
=
D-glucono-1,5-lactone
+
NAD(P)H
+
H+

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 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.47 glucose 1-dehydrogenase [NAD(P)+]

General Stability

General Stability on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.05% SDS, no loss of activity, 0.1%, slow decrease
-
2 M urea, 24 h, room temperature, no loss of activity, slow decrease at 4 M
-
4 M guanidinium chloride, rapid inactivation
-
4 M urea, room temperature, 6 h, 100% activity
-
crude enzyme loses 90% activity after 3 days at 5°C
-
enzyme shows good stability at low water content and at low salt concentration in reverse micelles
-
glucose dehydrogenase isoenzymes are stabilized in presence of 2 M NaCl. The effect is especially large for GlcDH-III, which is the most unstable enzyme
-
guanidinium chloride, mid-point of the denaturation curve is 0.65 or 0.63 M
-
H4-furan, rapid inactivation
-
NaCl stabilizes the enzyme at alkline pH and elevated temperatures
-
purified enzyme is indefinitely stable in the frozen state or in solution at pH 6.5 containing 3 M NaCl and a protein concentration of more than 0.5 mg/ml. Diluted enzyme solutions can be stabilized to the same degree by adding 0.5% polyvinylpyrrolidone. Any reduction of the ionic strength of enzyme solution leads to an irreversible inactivation which can be only partially prevented by additrion of polyvinylpyrrolidone
-
stability increases in the presence of glycerol
-
unfolding of the enzyme in 8 M urea is strongly inhibited by high concentrations of NaCl
-
unstable at low ionic strength, in 67 mM phosphate buffer enzyme activity decreases to 80% within 5 hours at pH 6.5 and 0.01 mg/ml protein, reduction to 57% at 40 mM phosphate, high concentration of NAD inhibit dissociation
-