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show all sequences of 1.1.1.121

Structural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase

Yasutake, Y.; Nishiya, Y.; Tamura, N.; Tamura, T.; J. Mol. Biol. 367, 1034-1046 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene aldT, overexpression of His-tagged enzyme in Escherichia coli strain BL21
Thermoplasma acidophilum
Crystallization (Commentary)
Crystallization
Organism
purified recombinant AldT in ligand-free form, in complex with NADH, and in complex with the substrate D-mannose, hanging drop or sitting drop vapor diffusion method, 20C, 8 mg/ml protein and 4 mM mM beta-NADH, mixing of 0.001-0.0025 ml of reservoir solution and sample solution, and equilibration against 0.5 ml of reservoir solution, streak-seeding method, from 0.1 M sodium acetate, pH 5.0, 0.2 M ammonium sulfate, 16% w/v PEG 3350, and 15% v/v glycerol, or from 0.1 M sodium acetate, pH 5.0-5.4, 0.2 M ammonium sulfate, 14-18% PEG 3350, and 15-20% glycerol, X-ray diffraction structure determination and analysis at 2.1 A, 1.65 A, and 1.6 A resolution, respectively, modelling
Thermoplasma acidophilum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-mannose + NAD+
Thermoplasma acidophilum
-
?
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermoplasma acidophilum
-
gene aldT
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21
Thermoplasma acidophilum
Reaction
Reaction
Commentary
Organism
D-aldose + NAD+ = D-aldonolactone + NADH + H+
catalytic mechanism involving a conserved catalytic triad Ser-Tyr-Lys at the catalytic site, the C-terminal tail shuts the substrate-binding pocket, overview
Thermoplasma acidophilum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-mannose + NAD+
-
688344
Thermoplasma acidophilum
?
-
-
-
r
D-mannose + NAD+
AldT is a unique enzyme that exhibits the highest dehydrogenase activity against D-mannose, the enzyme catalyzes the oxidation of several monosaccharides with a preference for NAD+ rather than NADP+ as a cofactor. Conformation of the Glu side-chain is crucial for discrimination between D-mannose and its C2 epimer D-glucose, and the conformation of the glutamate side-chain depends on the spatial arrangement of nearby hydrophobic residues that do not directly interact with the substrate, D-mannose recognition mechanism of AldT and inter-subunit interactions, overview
688344
Thermoplasma acidophilum
?
-
-
-
r
additional information
structural insights into substrate selectivity of AldT, overview
688344
Thermoplasma acidophilum
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
the AldT subunit forms a typical SDR fold with an unexpectedly long C-terminal tail and assembles into an intertwined tetramer, inter-subunit interactions, crystal structure, structure comparison, overview
Thermoplasma acidophilum
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
preference for NAD+ rather than NADP+ as a cofactor, binding site structure, overview
Thermoplasma acidophilum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene aldT, overexpression of His-tagged enzyme in Escherichia coli strain BL21
Thermoplasma acidophilum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
preference for NAD+ rather than NADP+ as a cofactor, binding site structure, overview
Thermoplasma acidophilum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant AldT in ligand-free form, in complex with NADH, and in complex with the substrate D-mannose, hanging drop or sitting drop vapor diffusion method, 20C, 8 mg/ml protein and 4 mM mM beta-NADH, mixing of 0.001-0.0025 ml of reservoir solution and sample solution, and equilibration against 0.5 ml of reservoir solution, streak-seeding method, from 0.1 M sodium acetate, pH 5.0, 0.2 M ammonium sulfate, 16% w/v PEG 3350, and 15% v/v glycerol, or from 0.1 M sodium acetate, pH 5.0-5.4, 0.2 M ammonium sulfate, 14-18% PEG 3350, and 15-20% glycerol, X-ray diffraction structure determination and analysis at 2.1 A, 1.65 A, and 1.6 A resolution, respectively, modelling
Thermoplasma acidophilum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-mannose + NAD+
Thermoplasma acidophilum
-
?
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21
Thermoplasma acidophilum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-mannose + NAD+
-
688344
Thermoplasma acidophilum
?
-
-
-
r
D-mannose + NAD+
AldT is a unique enzyme that exhibits the highest dehydrogenase activity against D-mannose, the enzyme catalyzes the oxidation of several monosaccharides with a preference for NAD+ rather than NADP+ as a cofactor. Conformation of the Glu side-chain is crucial for discrimination between D-mannose and its C2 epimer D-glucose, and the conformation of the glutamate side-chain depends on the spatial arrangement of nearby hydrophobic residues that do not directly interact with the substrate, D-mannose recognition mechanism of AldT and inter-subunit interactions, overview
688344
Thermoplasma acidophilum
?
-
-
-
r
additional information
structural insights into substrate selectivity of AldT, overview
688344
Thermoplasma acidophilum
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
the AldT subunit forms a typical SDR fold with an unexpectedly long C-terminal tail and assembles into an intertwined tetramer, inter-subunit interactions, crystal structure, structure comparison, overview
Thermoplasma acidophilum
Other publictions for EC 1.1.1.121
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)
697263
Asada
Biochemical and structural cha ...
Thermus thermophilus HB8
Chem. Biol. Interact.
178
117-126
2009
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688344
Yasutake
Structural insights into uniqu ...
Thermoplasma acidophilum
J. Mol. Biol.
367
1034-1046
2007
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718488
Yasutake
Crystallization and preliminar ...
Thermoplasma acidophilum
Acta Crystallogr. Sect. F
62
586-589
2006
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Nishiya
Analysis of bacterial glucose ...
Thermoplasma acidophilum
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5692
Green
Carbohydrate metabolism in som ...
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31-34
1984
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285794
Dahms
D-Fucose metabolism in a pseud ...
Pseudomonas sp., Pseudomonas sp. MSU-1
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2222-2227
1972
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285790
Cline
The isolation of three sugar d ...
Pseudomonas sp., Pseudomonas sp. G6
J. Biol. Chem.
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4488-4492
1965
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Cline
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285797
Cline
Some physical properties of th ...
Pseudomonas sp., Pseudomonas sp. G6
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1965
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