BRENDA - Enzyme Database show
show all sequences of 4.2.1.46

Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase: identification and preliminary characterization of functional amino acid residues at the active site

Hegeman, A.D.; Gross, J.W.; Frey, P.A.; Biochemistry 40, 6598-6610 (2001)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Inhibitors
Commentary
Organism
Structure
dTDP-galactose
-
Escherichia coli
dTDP-xylose
-
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187A
Escherichia coli
0.0015
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187S
Escherichia coli
0.0033
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232A
Escherichia coli
0.005
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232N
Escherichia coli
0.0055
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190A
Escherichia coli
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 D135A
Escherichia coli
0.0073
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190H
Escherichia coli
0.0079
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N
Escherichia coli
0.008
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232Q; pH 7.5, 37°C, mutant enzyme K199M
Escherichia coli
0.009
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136Q
Escherichia coli
0.011
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E198Q
Escherichia coli
0.012
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136A
Escherichia coli
0.013
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme K199R
Escherichia coli
0.019
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N/E136Q
Escherichia coli
0.025
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190D
Escherichia coli
0.031
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme Y301F
Escherichia coli
2.2
-
dTDP-glucose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
30
-
UDP-glucose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P27830
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dTDP-glucose
-
650072
Escherichia coli
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
650072
Escherichia coli
?
UDP-D-glucose
-
650072
Escherichia coli
UDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0089
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190A
Escherichia coli
0.011
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190D
Escherichia coli
0.017
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136A; pH 7.5, 37°C, mutant enzyme K199R
Escherichia coli
0.019
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E198Q
Escherichia coli
0.022
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135A
Escherichia coli
0.0226
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190H
Escherichia coli
0.024
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N/E136Q
Escherichia coli
0.024
-
UDP-glucose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
0.0395
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N
Escherichia coli
0.042
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme Y301F
Escherichia coli
0.0425
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme K199M
Escherichia coli
0.043
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232Q
Escherichia coli
0.073
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136Q
Escherichia coli
0.085
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232A
Escherichia coli
0.52
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187A
Escherichia coli
0.72
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232N
Escherichia coli
1.2
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187S
Escherichia coli
1.9
-
dTDP-glucose
pH 7.5, 18°C, wild-type enzyme
Escherichia coli
4.9
-
dTDP-glucose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
6.08
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187A; pH 7.5, 37°C, mutant enzyme H232N
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
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]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0112
-
dTDP-xylose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
0.097
-
dTDP-galactose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
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
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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 (protein specific)
Inhibitors
Commentary
Organism
Structure
dTDP-galactose
-
Escherichia coli
dTDP-xylose
-
Escherichia coli
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0112
-
dTDP-xylose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
0.097
-
dTDP-galactose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.001
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187A
Escherichia coli
0.0015
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187S
Escherichia coli
0.0033
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232A
Escherichia coli
0.005
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232N
Escherichia coli
0.0055
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190A
Escherichia coli
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 D135A
Escherichia coli
0.0073
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190H
Escherichia coli
0.0079
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N
Escherichia coli
0.008
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232Q; pH 7.5, 37°C, mutant enzyme K199M
Escherichia coli
0.009
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136Q
Escherichia coli
0.011
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E198Q
Escherichia coli
0.012
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136A
Escherichia coli
0.013
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme K199R
Escherichia coli
0.019
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N/E136Q
Escherichia coli
0.025
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190D
Escherichia coli
0.031
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme Y301F
Escherichia coli
2.2
-
dTDP-glucose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
30
-
UDP-glucose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dTDP-glucose
-
650072
Escherichia coli
dTDP-4-dehydro-6-deoxy-D-glucose + H2O
-
650072
Escherichia coli
?
UDP-D-glucose
-
650072
Escherichia coli
UDP-4-dehydro-6-deoxy-D-glucose + H2O
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0089
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190A
Escherichia coli
0.011
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190D
Escherichia coli
0.017
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136A; pH 7.5, 37°C, mutant enzyme K199R
Escherichia coli
0.019
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E198Q
Escherichia coli
0.022
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135A
Escherichia coli
0.0226
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme N190H
Escherichia coli
0.024
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N/E136Q
Escherichia coli
0.024
-
UDP-glucose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
0.0395
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme D135N
Escherichia coli
0.042
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme Y301F
Escherichia coli
0.0425
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme K199M
Escherichia coli
0.043
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232Q
Escherichia coli
0.073
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme E136Q
Escherichia coli
0.085
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232A
Escherichia coli
0.52
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187A
Escherichia coli
0.72
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme H232N
Escherichia coli
1.2
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187S
Escherichia coli
1.9
-
dTDP-glucose
pH 7.5, 18°C, wild-type enzyme
Escherichia coli
4.9
-
dTDP-glucose
pH 7.5, 37°C, wild-type enzyme
Escherichia coli
6.08
-
dTDP-glucose
pH 7.5, 37°C, mutant enzyme C187A; pH 7.5, 37°C, mutant enzyme H232N
Escherichia coli
Other publictions for EC 4.2.1.46
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
747917
Li
Characterization of the dTDP- ...
Campylobacter jejuni
Glycobiology
27
358-369
2017
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
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A 96-well microtiter plate as ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Identification of a dTDP-rham ...
Caenorhabditis elegans
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Identification of elaiophylin ...
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729054
Chen
Distribution of dTDP-glucose-4 ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 5187, Dietzia sp. 3149, Dietzia sp. DQ12-45-1b 3149, Ensifer sp. AS08, Ensifer sp. AS08 448, Filomicrobium sp. 454, Glycomyces sp. 3338, Micromonospora sp. 114, Micromonospora sp., Micromonospora sp. 282, Micromonospora sp. 3113, Micromonospora sp. 3134, Micromonospora sp. 3137, Micromonospora sp. 3191, Micromonospora sp. 3372-2, Micromonospora sp. 3387, Micromonospora sp. 3437-1, Micromonospora sp. 5297, Nocardia sp., Nocardia sp. 5314, Prauseria sp. 3425, Pseudomonas sp., Pseudomonas sp. 5302, Rhodococcus sp., Rhodococcus sp. 3376-1, Rhodospirillaceae bacterium 5305, Saccharothrix sp. 5133, Shimazuella sp. 3435, Streptomyces sp., Streptomyces sp. 3127, Streptomyces sp. 3419, Streptomyces sp. 5175, Streptomyces sp. 5191, Streptomyces sp. 5311, Streptomyces sp. 5320, Streptomyces sp. 568, Streptomyces sp. SCC 2136, Streptosporangium sp., Streptosporangium sp. 5322, Verrucosispora sp. 3133
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Precursor for biosynthesis of ...
Streptomyces peucetius
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Parakkottil Chothi
Identification of an L-rhamnos ...
Acanthamoeba polyphaga Mimivirus, Acanthocystis turfacea chlorella virus 1
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8829-8838
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690812
Pfoestl
Biosynthesis of dTDP-3-acetami ...
Thermoanaerobacterium thermosaccharolyticum, Thermoanaerobacterium thermosaccharolyticum E207-71
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410
187-194
2008
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Allard
High resolution X-ray structur ...
Streptomyces venezuelae
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279
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Du
Identification and functional ...
Streptoalloteichus tenebrarius
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49
99-107
2004
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650136
Hegeman
Concerted and stepwise dehydra ...
Escherichia coli
Biochemistry
41
2797-2804
2002
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2
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652770
Sohng
-
Function of lysine-148 in dTDP ...
Streptomyces antibioticus, Streptomyces antibioticus Tue99
J. Microbiol. Biotechnol.
12
217-221
2002
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650028
Gross
Dehydration is catalyzed by gl ...
Escherichia coli
Biochemistry
40
12497-12504
2001
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9
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19
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650072
Hegeman
Probing catalysis by Escherich ...
Escherichia coli
Biochemistry
40
6598-6610
2001
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17
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2
19
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20
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650089
Gerratana
Mechanistic roles of Thr134, T ...
Escherichia coli
Biochemistry
40
9187-9195
2001
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7
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8
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Allard
The crystal structure of dTDP- ...
Salmonella enterica
J. Mol. Biol.
307
283-295
2001
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1
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649133
Allard
The purification, crystallizat ...
Salmonella enterica
Acta Crystallogr. Sect. D
56
222-225
2000
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1
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649934
Gross
Characterization of enzymatic ...
Escherichia coli
Biochemistry
39
13633-13640
2000
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652771
Yoo
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Expression of orf7(oxi III) as ...
Streptomyces antibioticus, Streptomyces antibioticus Tu99
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9
206-212
1999
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2
1
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5725
Stein
Combined preparative enzymatic ...
Salmonella enterica subsp. enterica serovar Typhimurium
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15
139-145
1998
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1
-
1
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5724
Naundorf
Substrate specificity of nativ ...
Escherichia coli
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1
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3
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3
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5723
Linton
Cloning of the genes encoding ...
Saccharopolyspora erythraea
Gene
153
33-40
1995
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1
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5726
Thompson
Purification and characterizat ...
Streptomyces peucetius, Streptomyces sp. C5
J. Gen. Microbiol.
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779-786
1992
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5722
Romana
High level expression and puri ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochem. Biophys. Res. Commun.
174
846-852
1991
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5712
Vara
Purification of thymidine-diph ...
Saccharopolyspora erythraea
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263
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1988
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5713
Matern
Stoffwechselprodukte von Mikro ...
Streptomyces rimosus
Arch. Mikrobiol.
88
37-48
1973
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3
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5714
Glaser
-
Dehydration in nucleotide-link ...
Escherichia coli
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
465-480
1971
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5715
Zarkowsky
The mechanism of 6-deoxyhexose ...
Escherichia coli
J. Biol. Chem.
245
6599-6606
1970
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2
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5716
Zarkowsky
The mechanism of 6-deoxyhexose ...
Escherichia coli
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38
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1970
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1
-
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1
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
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-
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-
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-
-
5717
Wang
Biological mechanisms involved ...
Escherichia coli
J. Biol. Chem.
245
8-14
1970
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
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-
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-
2
-
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-
-
-
-
-
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1
-
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1
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1
-
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-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
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-
5718
Zarkowsky
The mechanism of 6-deoxyhexose ...
Escherichia coli
J. Biol. Chem.
244
4750-4756
1969
-
-
-
-
-
-
2
2
-
-
1
1
-
1
-
-
1
-
-
-
1
-
3
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
-
-
2
-
2
-
-
1
1
-
-
-
1
-
-
1
-
3
-
-
-
-
-
1
1
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5719
Wang
Biological mechanisms involved ...
Escherichia coli
J. Biol. Chem.
244
3430-3437
1969
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-
-
1
-
-
2
1
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1
1
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1
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1
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1
1
2
-
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1
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1
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1
1
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2
-
1
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-
1
1
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-
-
1
-
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1
1
2
-
-
-
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-
1
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-
5720
Melo
The mechanism of 6-deoxyhexose ...
Escherichia coli
J. Biol. Chem.
243
1467-1474
1968
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-
-
-
-
-
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1
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1
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1
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1
2
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1
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1
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1
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1
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1
2
-
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-
5721
Gilbert
Thymidine diphosphate 4-acetam ...
Escherichia coli
J. Biol. Chem.
240
1305-1308
1965
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1
2
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1
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1
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1
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1
2
2
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1
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1
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1
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1
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2
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1
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1
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1
2
2
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1
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