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1.1.1.121: aldose 1-dehydrogenase (NAD+)

This is an abbreviated version!
For detailed information about aldose 1-dehydrogenase (NAD+), go to the full flat file.

Word Map on EC 1.1.1.121

Reaction

D-aldose
+
NAD+
=
D-aldonolactone
 +
NADH
 +
H+

Synonyms

aldohexose dehydrogenase, aldose dehydrogenase, aldose-1-dehydrogenase, AldT, D-aldohexose dehydrogenase, dehydrogenase, D-aldohexose, More, Ta0754, TAD, TTHA0369

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.121 aldose 1-dehydrogenase (NAD+)

Crystallization

Crystallization on EC 1.1.1.121 - aldose 1-dehydrogenase (NAD+)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion technique at 20°C under several acidic conditions with polyethylene glycol and ammonium sulfate as precipitants. Optimization of the initial crystallizations conditions yields single crystals in solution containing 0.1 M sodium acetate pH 4.6, 18%(w/v) PEG 4000, 0.2 M ammonium sulfate and 15%(v/v) glycerol. An X-ray diffraction data set is collected to a resolution of 2.8 A
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
-
oil-microbatch method, crystal structure of the enzyme-NAD+ binary complex at 1.65 A resolution. The structure provides evidence for the strict coenzyme specificity and broad substrate specificity of the enzyme
by oil-microbatch method, at 1.65 A resolution. TAD follows an ordered sequential mechanism in which the coenzyme binds first