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Literature summary 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

EC Number Protein Variants Comment Organism
4.2.1.46 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
4.2.1.46 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

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

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.46 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

EC Number Cofactor Comment Organism Structure
4.2.1.46 NAD+ tightly bound coenzyme Escherichia coli