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.

Search for more literature for 1.1.1.121

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

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	-	?	-	r

Organism

Organism	UniProt	Comment	Textmining
Thermoplasma acidophilum	-	gene aldT	-

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	a

Substrates and Products (Substrate)

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

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	-	Thermoplasma acidophilum
D-aldohexose dehydrogenase	-	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