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Literature summary for 1.1.1.47 extracted from

  • Froeschle, M.; Ulmer, W.; Jany, K.D.
    Tyrosine modification of glucose dehydrogenase from Bacillus megaterium. Effect of tetranitromethane on the enzyme in the tetrameric and monomeric state (1984), Eur. J. Biochem., 142, 533-540.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Tetranitromethane the rapid inactivation can be prevented by the presence of NAD, AMP, or ATP Priestia megaterium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
4 * 30000, gel filtration Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium P40288
-
-
Priestia megaterium IWG3 P40288
-
-

Purification (Commentary)

Purification (Comment) Organism
Sephadex G-100 gel filtration Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + NAD(P)+
-
Priestia megaterium D-glucono-1,5-lactone + NAD(P)H
-
?
D-glucose + NAD(P)+
-
Priestia megaterium IWG3 D-glucono-1,5-lactone + NAD(P)H
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 30000, gel filtration Priestia megaterium

Synonyms

Synonyms Comment Organism
glucose dehydrogenase
-
Priestia megaterium

pH Stability

pH Stability pH Stability Maximum Comment Organism
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 Priestia megaterium

Cofactor

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