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Literature summary for 4.2.1.46 extracted from

  • Gerratana, B.; Cleland, W.W.; Frey, P.A.
    Mechanistic roles of Thr134, Tyr160, and Lys 164 in the reaction catalyzed by dTDP-glucose 4,6-dehydratase (2001), Biochemistry, 40, 9187-9195.
    View publication on PubMed
Search for more literature for 4.2.1.46

Protein Variants

Protein Variants Comment Organism
K164A 15fold increase in Km-value for dTDP-glucose, 820fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 34fold decrease in turnover-number for dTDP-glucose Escherichia coli
K164M 8.7fold increase in Km-value for dTDP-glucose, 837fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 96fold decrease in turnover-number for dTDP-glucose Escherichia coli
T134A 1.2fold increase in Km-value for dTDP-glucose, 283fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 233fold decrease in turnover-number for dTDP-glucose Escherichia coli
T134S 3.7fold increase in Km-value for dTDP-glucose, 7.5fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 2fold decrease in turnover-number for dTDP-glucose Escherichia coli
T134V 3.3fold increase in Km-value for dTDP-glucose, 788fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 237fold decrease in turnover-number for dTDP-glucose Escherichia coli
Y160A 2.8fold increase in Km-value for dTDP-glucose, 683fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 247fold decrease in turnover-number for dTDP-glucose Escherichia coli
Y160F 1.2fold increase in Km-value for dTDP-glucose, 234fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 190fold decrease in turnover-number for dTDP-glucose Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
 dTDP-glucose pH 7.5, 37°C, wild-type enzyme Escherichia coli
0.007
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme T134A Escherichia coli
0.0073
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme Y160F Escherichia coli
0.017
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme Y160A Escherichia coli
0.02
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme T134V Escherichia coli
0.022
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme T134S Escherichia coli
0.052
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme K164M Escherichia coli
0.09
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme K164A Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P27830
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dTDP-glucose
-
 Escherichia coli dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0198
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme Y160A Escherichia coli
0.0207
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme T134V Escherichia coli
0.021
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme T134A Escherichia coli
0.0258
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme Y160F Escherichia coli
0.051
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme K164M Escherichia coli
0.14
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme K164A Escherichia coli
2.4
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme T134S Escherichia coli
4.9
-
 dTDP-glucose pH 7.5, 37°C, wild-type enzyme Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADH purified enzyme contains coenzyme in the reduced form. The bound NADH is oxidized to NAD+ by adding dTDP-4-keto-6-deoxyglucose. When all the coenzyme is in the oxidized form, the dTDP-sugars remove from the enzyme. In the Y160A variant, almost 98% of the coenzyme is tightly bound NADH. Variants K164M, T134V and Y160F contain 62%, 56% and 35% of bound NADH respectively Escherichia coli