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Literature summary extracted from

  • Yamamot, K.; Nagao, T.; Makino, Y.; Urabe, I.; Okada, H.
    Characterization of mutant glucose dehydrogenase with increasing stability (1990), Ann. N. Y. Acad. Sci., 613, 362-365.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.47 E96K mutant enzyme Priestia megaterium

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.47 E96A mutation increases thermostability at pH 6.5 Priestia megaterium
1.1.1.47 E96G mutation increases thermostability at pH 6.5 Priestia megaterium
1.1.1.47 E96K mutation increases thermostability by about 15°C at pH 6.5 Priestia megaterium
1.1.1.47 Q252L mutation increases thermostability at pH 6.5 Priestia megaterium
1.1.1.47 Y253C mutation increases thermostability at pH 6.5 Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.47 0.0051
-
NADP+ E96K mutant Priestia megaterium
1.1.1.47 0.0076
-
NADP+ E96G mutant Priestia megaterium
1.1.1.47 0.0093
-
NADP+ E96A mutant Priestia megaterium
1.1.1.47 0.018
-
NAD+ E96K mutant Priestia megaterium
1.1.1.47 0.026
-
NADP+ Q252L mutant Priestia megaterium
1.1.1.47 0.027
-
NADP+ wild type Priestia megaterium
1.1.1.47 0.037
-
NADP+ Y253C mutant Priestia megaterium
1.1.1.47 0.17
-
NAD+ E96G mutant Priestia megaterium
1.1.1.47 0.19
-
NAD+ Q252L mutant Priestia megaterium
1.1.1.47 0.25
-
NAD+ Y253C mutant Priestia megaterium
1.1.1.47 0.31
-
NAD+ E96A mutant Priestia megaterium
1.1.1.47 0.37
-
NAD+ wild type Priestia megaterium
1.1.1.47 2.7
-
beta-D-glucose E96K mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 4
-
beta-D-glucose E96K mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 8.7
-
beta-D-glucose E96A mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 9
-
beta-D-glucose Q252L mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 9.5
-
beta-D-glucose wild type, coenzyme NAD+ Priestia megaterium
1.1.1.47 10
-
beta-D-glucose Q252L mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 11
-
beta-D-glucose wild type, coenzyme NADP+ Priestia megaterium
1.1.1.47 13
-
beta-D-glucose E96A mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 16
-
beta-D-glucose E96G mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 18
-
beta-D-glucose E96G mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 55
-
beta-D-glucose Y253C mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 85
-
beta-D-glucose Y253C mutant, coenzyme NADP+ 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 beta-D-glucose + NADP+
-
Priestia megaterium D-glucono-1,5-lactone + NADPH + H+
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.47 40
-
pH 6.5, 20 min, wild-type enzyme is stable Priestia megaterium
1.1.1.47 50
-
pH 6.5, 20 min, complete inactivation of wild-type enzyme, mutant enzyme E96K, E96G, E96A, Q252L and Y253C are stable Priestia megaterium
1.1.1.47 55
-
pH 6.5, 20 min, about 65% loss of acticity of mutant enzyme Y253C, about 20% loss of activity of mutant enzyme Y252L, mutant enzyme E96K, E96G and E96A are stable Priestia megaterium
1.1.1.47 60
-
pH 6.5, 20 min, complete loss of activity of enzyme Y253C about 95% loss of activity of mutant enzyme Y252L, about 30% loss of activity of mutant enzyme E96G, mutant enzymes E96K and E95A are stable Priestia megaterium
1.1.1.47 65
-
pH 6.5, 20 min, complete loss of activity of mutant enzyme Q252L, about 50% loss of activity of mutant enzyme E96K, about 10% loss of activity of mutant enzyme E96A 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 18
-
beta-D-glucose E96K mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 18
-
NADP+ E96K mutant Priestia megaterium
1.1.1.47 23
-
NAD+ E96K mutant Priestia megaterium
1.1.1.47 23
-
beta-D-glucose E96K mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 92
-
beta-D-glucose E96G mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 92
-
NADP+ E96G mutant Priestia megaterium
1.1.1.47 97
-
NAD+ E96A mutant Priestia megaterium
1.1.1.47 97
-
beta-D-glucose E96A mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 98
-
beta-D-glucose E96A mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 98
-
NADP+ E96A mutant Priestia megaterium
1.1.1.47 114
-
NAD+ E96G mutant Priestia megaterium
1.1.1.47 114
-
beta-D-glucose E96G mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 186
-
beta-D-glucose Y253C mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 186
-
NADP+ Y253C mutant Priestia megaterium
1.1.1.47 200
-
NAD+ Y253C mutant Priestia megaterium
1.1.1.47 200
-
beta-D-glucose Y253C mutant, coenzyme NAD+ Priestia megaterium
1.1.1.47 260
-
NADP+ wild type Priestia megaterium
1.1.1.47 260
-
beta-D-glucose wild type, coenzyme NADP+ Priestia megaterium
1.1.1.47 300
-
beta-D-glucose Q252L mutant, coenzyme NADP+ Priestia megaterium
1.1.1.47 300
-
NADP+ Q252L mutant Priestia megaterium
1.1.1.47 390
-
NAD+ wild type, coenzyme NAD+ Priestia megaterium
1.1.1.47 390
-
beta-D-glucose wild type, coenzyme NAD+ Priestia megaterium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.47 4 8 30°C, 20 min, mutant enzyme Q252L is stable Priestia megaterium
1.1.1.47 4 10 30°C, 20 min, mutant enzymes E96K and E95A, less than 20% loss of activity Priestia megaterium
1.1.1.47 5
-
30°C, 20 min, about 55% loss of activity of mutant enzyme Y253C, about 35% loss of activity of mutant enzyme E96G and wild-type enzyme Priestia megaterium
1.1.1.47 6 7 30°C, 20 min, wild-type and mutant enzyme Y253C are stable Priestia megaterium
1.1.1.47 8
-
30°C, 20 min, about 50% loss of activity of mutant enzyme Y253C, about 80% loss of wild-type enzyme, about 30% loss of activity of mutant enzyme E96G and E96, about 15% loss of activity of mutant enzyme E96K Priestia megaterium

Cofactor

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