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Literature summary for 1.1.1.47 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
Search for more literature for 1.1.1.47

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
Q252L mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH Priestia megaterium
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]

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

Organism

Organism UniProt Comment Textmining
Priestia megaterium P40288
-
-
Priestia megaterium IGW3 P40288
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer gel filtration Priestia megaterium

Synonyms

Synonyms Comment Organism
GlcDH
-
 Priestia megaterium

Turnover Number [1/s]

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
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

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