The enzyme is involved in biosynthesis of L-colitose, a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides, where it catalyses the reaction in the reverse direction. The enzyme also performs the NAD(P)H-dependent epimerisation at C-5 of the sugar. The enzyme from Yersinia pseudotuberculosis is Si-specific with respect to NAD(P)H .
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The enzyme appears in viruses and cellular organisms
The enzyme is involved in biosynthesis of L-colitose, a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides, where it catalyses the reaction in the reverse direction. The enzyme also performs the NAD(P)H-dependent epimerisation at C-5 of the sugar. The enzyme from Yersinia pseudotuberculosis is Si-specific with respect to NAD(P)H [1].
bifunctional enzyme catalyzing the C-5 epimerization of GDP-4-dehydro-3,6-dideoxy-D-mannose and the subsequent C-4 keto reduction of the resulting L-epimer to give GDP-L-colitose
bifunctional enzyme catalyzing the C-5 epimerization of GDP-4-dehydro-3,6-dideoxy-D-mannose and the subsequent C-4 keto reduction of the resulting L-epimer to give GDP-L-colitose
the enzyme catalyzes the C-5 epimerization of GDP-4-dehydro-3,6-dideoxy-D-mannose and the subsequent C-4 keto reduction of the resulting L-epimer to give GDP-L-colitose. The stereochemical preference of ColC with regard to the transfer of one of the diastereotopic methylene hydrogens at C-4 of the dihydronicotinamide ring is established to be pro-S stereospecific
the enzyme catalyzes the C-5 epimerization of GDP-4-dehydro-3,6-dideoxy-D-mannose and the subsequent C-4 keto reduction of the resulting L-epimer to give GDP-L-colitose. The stereochemical preference of ColC with regard to the transfer of one of the diastereotopic methylene hydrogens at C-4 of the dihydronicotinamide ring is established to be pro-S stereospecific
Biosynthesis of colitose: expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-D-mannose-3-dehydrase (ColD) and GDP-L-colitose synthase (ColC)
Biochemistry
43
16450-16460
2004
Yersinia pseudotuberculosis, Yersinia pseudotuberculosis VIA