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Literature summary extracted from

  • Baik, S.H.; Michel, F.; Aghajari, N.; Haser, R.; Harayama, S.
    Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state (2005), Appl. Environ. Microbiol., 71, 3285-3293.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.47 expressed in Escherichia coli strain JM109 Priestia megaterium

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.47 E170K mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH Priestia megaterium
1.1.1.47 Q252L mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH Priestia megaterium
1.1.1.47 Q252L/E170K mutant exhibits increased pH stability (95% residual activity at pH 8-10.5) in the absence of NaCl Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.47 0.15
-
NAD+ apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 0.17
-
NAD+ apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 0.22
-
NAD+ apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 0.33
-
NAD+ apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 7.5
-
D-glucose apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 8
-
D-glucose apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 8.5
-
D-glucose apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 14
-
D-glucose apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.47 Priestia megaterium P40288
-
-
1.1.1.47 Priestia megaterium IGW3 P40288
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.47 high-pressure liquid chromatography Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.47 D-glucose + NAD+
-
Priestia megaterium D-glucono-1,5-lactone + NADH + H+
-
?
1.1.1.47 D-glucose + NAD+
-
Priestia megaterium IGW3 D-glucono-1,5-lactone + NADH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.47 tetramer gel filtration Priestia megaterium

Synonyms

EC Number Synonyms Comment Organism
1.1.1.47 GlcDH
-
Priestia megaterium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.47 317
-
D-glucose apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 334
-
D-glucose apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 352
-
D-glucose apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium
1.1.1.47 395
-
D-glucose apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C Priestia megaterium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.47 7 9 wild type GlcDH shows reversible dissociation-association between inactive monomers and active tetramers when the pH is shifted between 9 and 7 Priestia megaterium

Cofactor

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