EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.121 | gene aldT, overexpression of His-tagged enzyme in Escherichia coli strain BL21 | Thermoplasma acidophilum |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.121 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.121 | D-mannose + NAD+ | Thermoplasma acidophilum | - |
? | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.121 | Thermoplasma acidophilum | - |
gene aldT | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.121 | recombinant His-tagged enzyme from Escherichia coli strain BL21 | Thermoplasma acidophilum |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.1.1.121 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.121 | D-mannose + NAD+ | - |
Thermoplasma acidophilum | ? | - |
r | |
1.1.1.121 | 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 | |
1.1.1.121 | additional information | structural insights into substrate selectivity of AldT, overview | Thermoplasma acidophilum | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.121 | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.121 | AldT | - |
Thermoplasma acidophilum |
1.1.1.121 | D-aldohexose dehydrogenase | - |
Thermoplasma acidophilum |
1.1.1.121 | More | the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily | Thermoplasma acidophilum |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.121 | NAD+ | preference for NAD+ rather than NADP+ as a cofactor, binding site structure, overview | Thermoplasma acidophilum |