DTDP-glucose 4,6-dehydratase

DTDP-glucose 4,6-dehydratase
dTDP-glucose 4,6-dehydratase
Identifiers
EC number 4.2.1.46
CAS number 37259-54-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a dTDP-glucose 4,6-dehydratase (EC 4.2.1.46) is an enzyme that catalyzes the chemical reaction

dTDP-glucose \rightleftharpoons dTDP-4-dehydro-6-deoxy-D-glucose + H2O

Hence, this enzyme has one substrate, dTDP-glucose, and two products, dTDP-4-dehydro-6-deoxy-D-glucose and H2O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is dTDP-glucose 4,6-hydro-lyase (dTDP-4-dehydro-6-deoxy-D-glucose-forming). Other names in common use include thymidine diphosphoglucose oxidoreductase, TDP-glucose oxidoreductase, and dTDP-glucose 4,6-hydro-lyase. This enzyme participates in 4 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, polyketide sugar unit biosynthesis, and biosynthesis of vancomycin group antibiotics. It employs one cofactor, NAD+.

Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1BXK, 1G1A, 1KEP, 1KER, 1KET, 1KEU, 1KEW, 1OC2, 1R66, 1R6D, and 2HUN.

References

  • GILBERT JM, MATSUHASHI M, STROMINGER JL (1965). "THYMIDINE DIPHOSPHATE 4-ACETAMIDO-4,6-DIDEOXYHEXOSES. II PURIFICATION AND PROPERTIES OF THYMIDINE DIPHOSPHATE D-GLUCOSE OXIDOREDUCTASE". J. Biol. Chem. 240: 1305–8. PMID 14284740. 
  • Melo A, Elliott WH, Glaser L (1968). "The mechanism of 6-deoxyhexose synthesis. I. Intramolecular hydrogen transfer catalyzed by deoxythymidine diphosphate D-glucose oxidoreductase". J. Biol. Chem. 243 (7): 1467–74. PMID 4869560. 
  • Wang SF, Gabriel O (1969). "Biological mechanisms involved in the formation of deoxy sugars. V Isolation and crystallization of thymidine diphosphate-D-glucose oxidoreductase from Escherichia coli B". J. Biol. Chem. 244 (13): 3430–7. PMID 4307450. 
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