4.2.1.46: dTDP-glucose 4,6-dehydratase
This is an abbreviated version!
For detailed information about dTDP-glucose 4,6-dehydratase, go to the full flat file.
Word Map on EC 4.2.1.46
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4.2.1.46
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dtdp-l-rhamnose
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dtdp-4-keto-6-deoxy-d-glucose
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3,5-epimerase
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dtdp-4-dehydrorhamnose
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o-antigen
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deoxysugars
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dtmp
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thymidylyltransferase
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6-deoxyhexose
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peucetius
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analysis
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synthesis
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pharmacology
- 4.2.1.46
- dtdp-l-rhamnose
- dtdp-4-keto-6-deoxy-d-glucose
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3,5-epimerase
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dtdp-4-dehydrorhamnose
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o-antigen
-
deoxysugars
- dtmp
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thymidylyltransferase
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6-deoxyhexose
- peucetius
- analysis
- synthesis
- pharmacology
Reaction
Synonyms
DesIV, dTDP-D-glucose 4,6-dehydratase, dTDP-D-glucose oxidoreductase, dTDP-glucose-4,6-dehydratase, dTGD, RmbB, rml-2, RmlB, TDP-D-glucose 4,6-dehydratase, TDP-glucose oxidoreductase, TDPDH, Thymidine diphosphate D-glucose oxidoreductase, thymidine diphosphate-glucose 4,6-dehydratase, Thymidine diphospho-D-glucose 4,6-dehydratase, Thymidine diphosphoglucose oxidoreductase, UDP-D-glucose 4,6-dehydratase, Ugd
ECTree
4.2.1.46 dTDP-glucose 4,6-dehydrataseAdvanced search results
results (
results (Engineering
Engineering on EC 4.2.1.46 - dTDP-glucose 4,6-dehydratase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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
D135135N/E136Q
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 340fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 204fold lower than that of the wild-type enzyme
D135A
D135N
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
E136A
E136Q
E198Q
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
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
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
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
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
K199M
K199R
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
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
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
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
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
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
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
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
Y301F
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
D135A
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switch from a concerted to stepwise dehydration mechanism is due to the loss of control over the glucosyl C5C6 bond rotation in the active site
D135A
the steady-state rate of conversion of dTDP-6-fluoro-6-deoxyglucose to dTDP-4-keto-6-deoxyglucose is identical to that of wild-type. The turnover number for dTDP-6-fluoro-6-deoxyglucose is 1.5fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 223fold lower than that of the wild-type enzyme
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
D135N
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switch from a concerted to stepwise dehydration mechanism is due to the loss of control over the glucosyl C5C6 bond rotation in the active site
D135N
the steady-state rate of conversion of dTDP-6-fluoro-6-deoxyglucose to dTDP-4-keto-6-deoxyglucose is identical to that of wild-type. The turnover number for dTDP-6-fluoro-6-deoxyglucose is 1.2fold higher than that of the wild-type enzyme, the turnover number for dTDP-glucose is 124fold lower than that of the wild-type enzyme
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
E136A
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 690fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 288fold lower than that of the wild-type enzyme
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
E136Q
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 69fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 67fold lower than that of the wild-type enzyme
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
E198Q
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 190fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 258fold lower than that of the wild-type enzyme
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
K199M
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 260fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 115fold lower than that of the wild-type enzyme
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
K199R
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 680fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 288fold lower than that of the wild-type enzyme
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
Y301F
the turnover number for dTDP-6-fluoro-6-deoxyglucose is 31fold lower than that of the wild-type enzyme, the turnover number for dTDP-glucose is 117fold lower than that of the wild-type enzyme
