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Literature summary for 4.2.1.46 extracted from

  • Hegeman, A.D.; Gross, J.W.; Frey, P.A.
    Concerted and stepwise dehydration mechanisms observed in wild-type and mutated Escherichia coli dTDP-glucose 4,6-dehydratase (2002), Biochemistry, 41, 2797-2804.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D135A switch from a concerted to stepwise dehydration mechanism is due to the loss of control over the glucosyl C5–C6 bond rotation in the active site Escherichia coli
D135N switch from a concerted to stepwise dehydration mechanism is due to the loss of control over the glucosyl C5–C6 bond rotation in the active site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dTDP-glucose the conversion takes place in three steps: dehydrogenation to dTDP-4-ketoglucose, dehydration to dTDP-4-ketoglucose-5,6-ene and rereduction of C6 to the methyl group Escherichia coli dTDP-4-dehydro-6-deoxy-D-glucose + H2O
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Cofactor

Cofactor Comment Organism Structure
NAD+ tightly bound coenzyme Escherichia coli