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Literature summary for 1.1.1.121 extracted from

  • Yasutake, Y.; Nishiya, Y.; Tamura, N.; Tamura, T.
    Structural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase (2007), J. Mol. Biol., 367, 1034-1046.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene aldT, overexpression of His-tagged enzyme in Escherichia coli strain BL21 Thermoplasma acidophilum

Crystallization (Commentary)

Crystallization (Comment) 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, 20°C, 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-mannose + NAD+ Thermoplasma acidophilum
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?
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r

Organism

Organism UniProt Comment Textmining
Thermoplasma acidophilum
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gene aldT
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 Thermoplasma acidophilum

Reaction

Reaction Comment Organism Reaction ID
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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-mannose + NAD+
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Thermoplasma acidophilum ?
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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 Thermoplasma acidophilum ?
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r
additional information structural insights into substrate selectivity of AldT, overview Thermoplasma acidophilum ?
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?

Subunits

Subunits Comment 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

Synonyms

Synonyms Comment Organism
AldT
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Thermoplasma acidophilum
D-aldohexose dehydrogenase
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Thermoplasma acidophilum
More the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily Thermoplasma acidophilum

Cofactor

Cofactor Comment Organism Structure
NAD+ preference for NAD+ rather than NADP+ as a cofactor, binding site structure, overview Thermoplasma acidophilum