Literature summary for 4.2.1.46 extracted from

Gross, J.W.; Hegeman, A.D.; Vestling, M.M.; Frey, P.A.
Characterization of enzymatic processes by rapid mix-quench mass spectrometry: the case of dTDP-glucose 4,6-dehydratase (2000), Biochemistry, 39, 13633-13640.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P27830	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
dTDP-glucose	the single-turnover kinetic mechanism for the reaction is determined by rapid mix-chemical quench mass spectrometry. NAD+ initially oxidizes glucosyl C4 of dTDP-glucose to NADH and dTDP-4-ketoglucose. Next water is eliminated between C5 and C6 of dTDP-4-ketoglucose to form dTDP-4-ketoglucose-5,6-ene. Hydride transfer from NADH to C6 of dTDP-4-ketoglucose-5,6-ene regenerates NAD+ and produces the product dTDP-4-keto-4-deoxyglucose	Escherichia coli	dTDP-4-dehydro-6-deoxy-D-glucose + H2O	-	?

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Escherichia coli

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Release 2023.1 (January 2023)