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Literature summary 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

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.47 Priestia megaterium
-
-
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.1.1.47 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
1.1.1.47 More monomers, dimers and tetramers participate in aggregation equilibria which are dependent on enzyme and NaCl concentration and on the pH value Priestia megaterium
1.1.1.47 tetramer x-ray crystallography Priestia megaterium

Synonyms

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

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.47 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
1.1.1.47 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

EC Number Cofactor Comment Organism Structure
1.1.1.47 NAD+
-
 Priestia megaterium
1.1.1.47 NADP+
-
 Priestia megaterium