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Literature summary for 1.1.1.49 extracted from

  • Fuentealba, M.; Munoz, R.; Maturana, P.; Krapp, A.; Cabrera, R.
    Determinants of cofactor specificity for the glucose-6-phosphate dehydrogenase from Escherichia coli: simulation, kinetics and evolutionary studies (2016), PLoS ONE, 11, e0152403.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K18A the mutant with reduced catalytic efficiency shows 35fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold) Escherichia coli
K18A/R50A the mutant shows almost no activity Escherichia coli
K18T the mutant with reduced catalytic efficiency sshows 35fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold) Escherichia coli
R50A the mutant with reduced catalytic efficiency shows 50fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold) Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0075
-
NADP+ wild type enzyme, at pH 8.2 and 25°C Escherichia coli
0.099
-
NADP+ mutant enzyme K18A, at pH 8.2 and 25°C Escherichia coli
0.382
-
NADP+ mutant enzyme R50A, at pH 8.2 and 25°C Escherichia coli
2.477
-
NAD+ mutant enzyme K18A, at pH 8.2 and 25°C Escherichia coli
5.09
-
NAD+ wild type enzyme, at pH 8.2 and 25°C Escherichia coli
11.74
-
NAD+ mutant enzyme K18A/R50A, at pH 8.2 and 25°C Escherichia coli
14.66
-
NAD+ mutant enzyme R50A, at pH 8.2 and 25°C Escherichia coli
17.7
-
NADP+ mutant enzyme K18A/R50A, at pH 8.2 and 25°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose 6-phosphate + NADP+ Escherichia coli
-
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose 6-phosphate + NAD+ very low activity with NAD+ Escherichia coli 6-phospho-D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose 6-phosphate + NADP+
-
Escherichia coli 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?

Synonyms

Synonyms Comment Organism
G6PDH
-
Escherichia coli
glucose-6-phosphate dehydrogenase
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
109
-
NAD+ mutant enzyme K18A, at pH 8.2 and 25°C Escherichia coli
143
-
NADP+ mutant enzyme K18A, at pH 8.2 and 25°C Escherichia coli
165
-
NAD+ mutant enzyme K18A/R50A, at pH 8.2 and 25°C Escherichia coli
171
-
NAD+ mutant enzyme R50A, at pH 8.2 and 25°C Escherichia coli
174
-
NADP+ wild type enzyme, at pH 8.2 and 25°C Escherichia coli
185
-
NADP+ mutant enzyme K18A/R50A, at pH 8.2 and 25°C Escherichia coli
189
-
NADP+ mutant enzyme R50A, at pH 8.2 and 25°C Escherichia coli
288
-
NAD+ wild type enzyme, at pH 8.2 and 25°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADP+ the enzyme has strong preference towards NADP+ Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.001
-
NAD+ mutant enzyme K18A/R50A, at pH 8.2 and 25°C Escherichia coli
0.001
-
NADP+ mutant enzyme K18A/R50A, at pH 8.2 and 25°C Escherichia coli
0.01
-
NAD+ mutant enzyme R50A, at pH 8.2 and 25°C Escherichia coli
0.04
-
NAD+ mutant enzyme K18A, at pH 8.2 and 25°C Escherichia coli
0.06
-
NAD+ wild type enzyme, at pH 8.2 and 25°C Escherichia coli
500
-
NADP+ mutant enzyme R50A, at pH 8.2 and 25°C Escherichia coli
1400
-
NADP+ mutant enzyme K18A, at pH 8.2 and 25°C Escherichia coli
23200
-
NADP+ wild type enzyme, at pH 8.2 and 25°C Escherichia coli