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Literature summary for 1.1.1.47 extracted from

  • Maurer, e.; Pfleiderer, G.
    Reversible pH-induced dissociation of glucose dehydrogenase from Bacillus megaterium. II. Kinetics and mechanism (1987), Z. Naturforsch. C, 42, 907-915.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
NaCl reaction rate and dissociation at pH 9 are reduced by increasing the NaCl concentration (0-500 mM) Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + NAD+
-
Priestia megaterium D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NAD+
-
Priestia megaterium D-glucono-1,5-lactone + NADH + H+
-
?

Subunits

Subunits Comment Organism
More 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 Priestia megaterium
More monomers, dimers and tetramers participate in aggregation equilibria which are dependent on enzyme and NaCl concentration and on the pH value Priestia megaterium
tetramer x-ray crystallography Priestia megaterium

Synonyms

Synonyms Comment Organism
beta-D-glucose:NAD(P)+ 1-oxido-reductase
-
Priestia megaterium

pH Stability

pH Stability pH Stability Maximum Comment Organism
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 Priestia megaterium
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 Priestia megaterium

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Priestia megaterium
NADP+
-
Priestia megaterium