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Literature summary extracted from

  • Hegeman, A.D.; Gross, J.W.; Frey, P.A.
    Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase: identification and preliminary characterization of functional amino acid residues at the active site (2001), Biochemistry, 40, 6598-6610.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.46 C187A 9.4fold decrease in turnover number for dTDP-glucose compared to wild-type value, 6fold decrease in KM-value for dTDP-glucose compared to wild-type value. 8% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 C187S 4.1fold decrease in turnover number for dTDP-glucose compared to wild-type value, 4fold decrease in KM-value for dTDP-glucose compared to wild-type value. 5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 D135A 222fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.2fold increase in KM-value for dTDP-glucose compared to wild-type value. 30% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 D135N 124fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.3fold increase in KM-value for dTDP-glucose compared to wild-type value. 9% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 D135N/E136Q 204fold decrease in turnover number for dTDP-glucose compared to wild-type value, 3.2fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 E136A 288fold decrease in turnover number for dTDP-glucose compared to wild-type value, 2fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 E136Q 67fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.5fold increase in KM-value for dTDP-glucose compared to wild-type value. 3% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 E198Q 258fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.8fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 H232A 57.6fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.8fold decrease in KM-value for dTDP-glucose compared to wild-type value Escherichia coli
4.2.1.46 H232N 6.8fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.2fold decrease in KM-value for dTDP-glucose compared to wild-type value. 3% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 H232Q 114fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.3fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 K199M 115fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.3fold increase in KM-value for dTDP-glucose compared to wild-type value. 2% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 K199R 288fold decrease in turnover number for dTDP-glucose compared to wild-type value, 2.2fold increase in KM-value for dTDP-glucose compared to wild-type value. 2% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 N190A 551fold decrease in turnover number for dTDP-glucose compared to wild-type value, 0.92fold increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 N190D 441fold decrease in turnover number for dTDP-glucose compared to wild-type value, fold 4.2increase in KM-value for dTDP-glucose compared to wild-type value. Less than 0.5% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli
4.2.1.46 N190H 217fold decrease in turnover number for dTDP-glucose compared to wild-type value, 1.2fold increase in KM-value for dTDP-glucose compared to wild-type value Escherichia coli
4.2.1.46 Y301F 117fold decrease in turnover number for dTDP-glucose compared to wild-type value, 5.2fold increase in KM-value for dTDP-glucose compared to wild-type value. 39% of the mutant enzyme contains NADH during steady-state turnover by adding a large excess of dTDPglucose, compared to 45% of the wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.46 dTDP-galactose
-
 Escherichia coli
4.2.1.46 dTDP-xylose
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.46 0.001
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme C187A Escherichia coli
4.2.1.46 0.0015
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme C187S Escherichia coli
4.2.1.46 0.0033
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme H232A Escherichia coli
4.2.1.46 0.005
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme H232N Escherichia coli
4.2.1.46 0.0055
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme N190A Escherichia coli
4.2.1.46 0.006
-
 dTDP-glucose pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.2.1.46 0.007
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme D135A Escherichia coli
4.2.1.46 0.0073
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme N190H Escherichia coli
4.2.1.46 0.0079
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme D135N Escherichia coli
4.2.1.46 0.008
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme H232Q Escherichia coli
4.2.1.46 0.008
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme K199M Escherichia coli
4.2.1.46 0.009
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme E136Q Escherichia coli
4.2.1.46 0.011
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme E198Q Escherichia coli
4.2.1.46 0.012
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme E136A Escherichia coli
4.2.1.46 0.013
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme K199R Escherichia coli
4.2.1.46 0.019
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme D135N/E136Q Escherichia coli
4.2.1.46 0.025
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme N190D Escherichia coli
4.2.1.46 0.031
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme Y301F Escherichia coli
4.2.1.46 2.2
-
 dTDP-glucose pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.2.1.46 30
-
 UDP-glucose pH 7.5, 37°C, wild-type enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.46 Escherichia coli P27830
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.46
-
 Escherichia coli

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.46 0.0089
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme N190A Escherichia coli
4.2.1.46 0.011
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme N190D Escherichia coli
4.2.1.46 0.017
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme E136A Escherichia coli
4.2.1.46 0.017
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme K199R Escherichia coli
4.2.1.46 0.019
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme E198Q Escherichia coli
4.2.1.46 0.022
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme D135A Escherichia coli
4.2.1.46 0.0226
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme N190H Escherichia coli
4.2.1.46 0.024
-
 UDP-glucose pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.2.1.46 0.024
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme D135N/E136Q Escherichia coli
4.2.1.46 0.0395
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme D135N Escherichia coli
4.2.1.46 0.042
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme Y301F Escherichia coli
4.2.1.46 0.0425
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme K199M Escherichia coli
4.2.1.46 0.043
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme H232Q Escherichia coli
4.2.1.46 0.073
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme E136Q Escherichia coli
4.2.1.46 0.085
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme H232A Escherichia coli
4.2.1.46 0.52
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme C187A Escherichia coli
4.2.1.46 0.72
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme H232N Escherichia coli
4.2.1.46 1.2
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme C187S Escherichia coli
4.2.1.46 1.9
-
 dTDP-glucose pH 7.5, 18°C, wild-type enzyme Escherichia coli
4.2.1.46 4.9
-
 dTDP-glucose pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.2.1.46 6.08
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme C187A Escherichia coli
4.2.1.46 6.08
-
 dTDP-glucose pH 7.5, 37°C, mutant enzyme H232N Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.46 NADH 45% of the wild-type enzyme contains NADH during steady-state turnover for each variant by adding a large excess of dTDPglucose, 9% of mutant enzyme D135N, 30% of mutant enzyme D135A, 3% of mutant enzyme E136Q and H232N, 2% of mutant enzyme K199M and K199R, 39% of mutant enzyme Y301F, 8% of mutant enzyme C187A and less than 0.5% of mutant enzymes D135N/E136Q, E198Q, N190D, N190A and H232Q Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.1.46 0.0112
-
 dTDP-xylose pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.2.1.46 0.097
-
 dTDP-galactose pH 7.5, 37°C, wild-type enzyme Escherichia coli