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Literature summary extracted from

  • Alam, J.; Beyer, N.; Liu, H.W.
    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) (2004), Biochemistry, 43, 16450-16460.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.356
-
 Yersinia pseudotuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.356 0.075
-
 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose pH 7.5, 37°C, cosubstrate: NADPH Yersinia pseudotuberculosis
1.1.1.356 0.139
-
 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose pH 7.5, 37°C, cosubstrate: NADH Yersinia pseudotuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.356 35234
-
 2 * 35234, calculated from sequence Yersinia pseudotuberculosis
1.1.1.356 36000
-
 2 * 36000, SDS-PAGE Yersinia pseudotuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.356 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NAD(P)H + H+ Yersinia pseudotuberculosis the enzyme is involved in GDP-L-fucose biosynthesis. L-Colitose is a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides GDP-beta-L-colitose + NAD(P)+
-
 ?
1.1.1.356 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NAD(P)H + H+ Yersinia pseudotuberculosis VIA the enzyme is involved in GDP-L-fucose biosynthesis. L-Colitose is a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides GDP-beta-L-colitose + NAD(P)+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.356 Yersinia pseudotuberculosis
-
-
-
1.1.1.356 Yersinia pseudotuberculosis VIA
-
-
-
4.2.1.168 Yersinia pseudotuberculosis G4WJD4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.356 N-terminal His6-tagged ColC Yersinia pseudotuberculosis

Storage Stability

EC Number Storage Stability Organism
1.1.1.356 -80°C, stable for at least 6 months Yersinia pseudotuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.356 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NAD(P)H + H+ the enzyme is involved in GDP-L-fucose biosynthesis. L-Colitose is a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides Yersinia pseudotuberculosis GDP-beta-L-colitose + NAD(P)+
-
 ?
1.1.1.356 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NAD(P)H + H+ the enzyme is involved in GDP-L-fucose biosynthesis. L-Colitose is a 3,6-dideoxyhexose found in the O-antigen of Gram-negative lipopolysaccharides Yersinia pseudotuberculosis VIA GDP-beta-L-colitose + NAD(P)+
-
 ?
1.1.1.356 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NADH + H+ 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 Yersinia pseudotuberculosis GDP-beta-L-colitose + NAD+
-
 ?
1.1.1.356 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NADH + H+ 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 Yersinia pseudotuberculosis VIA GDP-beta-L-colitose + NAD+
-
 ?
1.1.1.356 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NADPH + H+ 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 Yersinia pseudotuberculosis GDP-beta-L-colitose + NADP+
-
 ?
1.1.1.356 GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NADPH + H+ 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 Yersinia pseudotuberculosis VIA GDP-beta-L-colitose + NADP+
-
 ?
4.2.1.168 GDP-4-dehydro-alpha-D-rhamnose + L-glutamate
-
 Yersinia pseudotuberculosis GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + 2-oxoglutarate + ammonia
-
 ?
4.2.1.168 additional information enzyme functions as GDP-4-keto-6-deoxy-D-mannose-3-dehydrase responsible for C-3 deoxygenation of GDP-4-keto-6-deoxy-D-mannose. The enzyme is coenzyme B6-dependent and catalysis is initiated by a transamination step in which pyridoxal 5'-phosphate is converted to pyridoxamine 5'-phosphate in the presene of L-glutamate. This coenzyme forms a Schiff base with the keto sugar substrate and the resulting adduct undergoes a pyridoxamine 5'-phosphate-mediated beta-dehydration reaction to give a sugar enamine intermediate, which after tautomerization and hydrolysis to release ammonia yields GDP-4-keto-3,6-dideoxy-D-mannose as the product Yersinia pseudotuberculosis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.356 homodimer 2 * 36000, SDS-PAGE Yersinia pseudotuberculosis
1.1.1.356 homodimer 2 * 35234, calculated from sequence Yersinia pseudotuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.356 ColC
-
 Yersinia pseudotuberculosis
4.2.1.168 colD
-
 Yersinia pseudotuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.356 37
-
 assay at Yersinia pseudotuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.356 7.5
-
 assay at Yersinia pseudotuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.356 NADH
-
 Yersinia pseudotuberculosis
1.1.1.356 NADPH
-
 Yersinia pseudotuberculosis