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
-
3,5-epimerase
-
dtdp-4-dehydrorhamnose
-
o-antigen
-
deoxysugars
- dtmp
-
thymidylyltransferase
-
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
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Cofactor
Cofactor on EC 4.2.1.46 - dTDP-glucose 4,6-dehydratase
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NAD+
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required as coenzyme, Lys138 does not play a role in the NAD-binding
NAD+
enzyme consists of an N-terminal NAD+ cofactor-binding domain and a C-terminal sugar-nucleotide binding domain
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
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