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Literature summary for 1.1.1.47 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)

Cloned (Comment) Organism
E96K mutant enzyme Priestia megaterium

Protein Variants

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
pH 6.5, 20 min, wild-type enzyme is stable Priestia megaterium
50
-
pH 6.5, 20 min, complete inactivation of wild-type enzyme, mutant enzyme E96K, E96G, E96A, Q252L and Y253C are stable Priestia megaterium
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
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
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]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
18
-
beta-D-glucose E96K mutant, coenzyme NADP+ Priestia megaterium
18
-
NADP+ E96K mutant Priestia megaterium
23
-
NAD+ E96K mutant Priestia megaterium
23
-
beta-D-glucose E96K mutant, coenzyme NAD+ Priestia megaterium
92
-
beta-D-glucose E96G mutant, coenzyme NADP+ Priestia megaterium
92
-
NADP+ E96G mutant Priestia megaterium
97
-
NAD+ E96A mutant Priestia megaterium
97
-
beta-D-glucose E96A mutant, coenzyme NAD+ Priestia megaterium
98
-
beta-D-glucose E96A mutant, coenzyme NADP+ Priestia megaterium
98
-
NADP+ E96A mutant Priestia megaterium
114
-
NAD+ E96G mutant Priestia megaterium
114
-
beta-D-glucose E96G mutant, coenzyme NAD+ Priestia megaterium
186
-
beta-D-glucose Y253C mutant, coenzyme NADP+ Priestia megaterium
186
-
NADP+ Y253C mutant Priestia megaterium
200
-
NAD+ Y253C mutant Priestia megaterium
200
-
beta-D-glucose Y253C mutant, coenzyme NAD+ Priestia megaterium
260
-
NADP+ wild type Priestia megaterium
260
-
beta-D-glucose wild type, coenzyme NADP+ Priestia megaterium
300
-
beta-D-glucose Q252L mutant, coenzyme NADP+ Priestia megaterium
300
-
NADP+ Q252L mutant Priestia megaterium
390
-
NAD+ wild type, coenzyme NAD+ Priestia megaterium
390
-
beta-D-glucose wild type, coenzyme NAD+ Priestia megaterium

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 8 30°C, 20 min, mutant enzyme Q252L is stable Priestia megaterium
4 10 30°C, 20 min, mutant enzymes E96K and E95A, less than 20% loss of activity Priestia megaterium
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
6 7 30°C, 20 min, wild-type and mutant enzyme Y253C are stable Priestia megaterium
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

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