1,3-propanediol dehydrogenase

This is an abbreviated version, for detailed information about 1,3-propanediol dehydrogenase, go to the full flat file.




(NADH)-linked 1,3-PD oxidoreductase, 1,3-PD dehydrogenase, 1,3-PD oxidoreductase, 1,3-PD-DH, 1,3-PD:NAD+ oxidoreductase, 1,3-Pdiol dehydrogenase, 1,3-propanediol dehydrogenase, 1,3-propanediol oxidoreductase, 1,3-propanediol-oxidoreductase, 1,3-propanediol:NAD oxidoreductase, 3-hydroxypropionaldehyde reductase, ADH3, dehydrogenase, 1,3-propanediol, DhaT, lr_0030, lr_1734, NADH-linked 1,3-propanediol oxidoreductase, PDOR, YqhD


     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
       1,3-propanediol dehydrogenase


Crystallization on EC - 1,3-propanediol dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
selenomethionine-labeled protein, to 2.4 A resolution. space group P32
by vapor diffusion in sitting drops at 20C, at 2.7 A resolution. The enzyme shows a decameric structure, formed by a pentamer of dimers, which is the catalytic form of the enzyme. Dimers are associated by strong ionic interactions that are responsible for the highly stable in vivo packing of the enzyme. The decameric arrangement is related to the cooperativity between monomers
homology modeling with cofactors NADH and NADPH
purified recombinant His-tagged enzyme, sitting-drop vapour diffusion, 22C, 0.0015 ml of 55 mg/ml protein in 50 mM HEPES, pH 7.4, 150 mM NaCl, 1 mM MnCl2 and 2 mM DTT, is mixed with an equal volume of reservoir solution containing 0.1 M MES, pH 6.5, with 12% w/v PEG 20000, and 10 mM CaCl2, 8-24 h, X-ray diffraction structure determination and analysis at 2.7 A resolution
to 3.2 A resolution. The electron density map around the active site shows no sign of a bound co-factor, but the active site metal could be located and identified as Ni2+
purified recombinant His-tagged protein in 20 mM Tris, pH 7.9, 150 mM NaCl, 0.25 mM TCEP, by nandroplet vapour diffusion method, cyrstallization buffer contains 20% PEG 300, 5% w/v PEG 8000, 10% glycerol, and 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis at 1.3 A resolution, modeling of 2 enzyme molecules, residues 1-359, complexed with 2 molecules of NADP+, 2 ions of Fe2+, 2 molecules of Tris, and 895 water molecules