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show all sequences of 1.1.1.356

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)

Alam, J.; Beyer, N.; Liu, H.W.; Biochemistry 43, 16450-16460 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Yersinia pseudotuberculosis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.075
-
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
pH 7.5, 37°C, cosubstrate: NADPH
Yersinia pseudotuberculosis
0.139
-
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
pH 7.5, 37°C, cosubstrate: NADH
Yersinia pseudotuberculosis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35234
-
2 * 35234, calculated from sequence
Yersinia pseudotuberculosis
36000
-
2 * 36000, SDS-PAGE
Yersinia pseudotuberculosis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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)+
-
-
?
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Yersinia pseudotuberculosis
-
-
-
Yersinia pseudotuberculosis VIA
-
-
-
Purification (Commentary)
Commentary
Organism
N-terminal His6-tagged ColC
Yersinia pseudotuberculosis
Storage Stability
Storage Stability
Organism
-80°C, stable for at least 6 months
Yersinia pseudotuberculosis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
721596
Yersinia pseudotuberculosis
GDP-beta-L-colitose + NAD(P)+
-
-
-
?
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
721596
Yersinia pseudotuberculosis VIA
GDP-beta-L-colitose + NAD(P)+
-
-
-
?
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
721596
Yersinia pseudotuberculosis
GDP-beta-L-colitose + NAD+
-
-
-
?
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
721596
Yersinia pseudotuberculosis VIA
GDP-beta-L-colitose + NAD+
-
-
-
?
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
721596
Yersinia pseudotuberculosis
GDP-beta-L-colitose + NADP+
-
-
-
?
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
721596
Yersinia pseudotuberculosis VIA
GDP-beta-L-colitose + NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 35234, calculated from sequence; 2 * 36000, SDS-PAGE
Yersinia pseudotuberculosis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Yersinia pseudotuberculosis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Yersinia pseudotuberculosis
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Yersinia pseudotuberculosis
NADPH
-
Yersinia pseudotuberculosis
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Yersinia pseudotuberculosis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Yersinia pseudotuberculosis
NADPH
-
Yersinia pseudotuberculosis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.075
-
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
pH 7.5, 37°C, cosubstrate: NADPH
Yersinia pseudotuberculosis
0.139
-
GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose
pH 7.5, 37°C, cosubstrate: NADH
Yersinia pseudotuberculosis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35234
-
2 * 35234, calculated from sequence
Yersinia pseudotuberculosis
36000
-
2 * 36000, SDS-PAGE
Yersinia pseudotuberculosis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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)+
-
-
?
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)+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
N-terminal His6-tagged ColC
Yersinia pseudotuberculosis
Storage Stability (protein specific)
Storage Stability
Organism
-80°C, stable for at least 6 months
Yersinia pseudotuberculosis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
721596
Yersinia pseudotuberculosis
GDP-beta-L-colitose + NAD(P)+
-
-
-
?
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
721596
Yersinia pseudotuberculosis VIA
GDP-beta-L-colitose + NAD(P)+
-
-
-
?
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
721596
Yersinia pseudotuberculosis
GDP-beta-L-colitose + NAD+
-
-
-
?
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
721596
Yersinia pseudotuberculosis VIA
GDP-beta-L-colitose + NAD+
-
-
-
?
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
721596
Yersinia pseudotuberculosis
GDP-beta-L-colitose + NADP+
-
-
-
?
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
721596
Yersinia pseudotuberculosis VIA
GDP-beta-L-colitose + NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 35234, calculated from sequence; 2 * 36000, SDS-PAGE
Yersinia pseudotuberculosis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Yersinia pseudotuberculosis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Yersinia pseudotuberculosis
Other publictions for EC 1.1.1.356
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
721596
Alam
Biosynthesis of colitose: expr ...
Yersinia pseudotuberculosis, Yersinia pseudotuberculosis VIA
Biochemistry
43
16450-16460
2004
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1
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2
-
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2
2
-
3
-
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1
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1
6
1
1
-
-
-
1
-
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2
-
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-
1
2
-
-
-
-
-
-
2
-
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2
2
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1
-
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1
6
1
1
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1
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-
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