1.1.1.202: 1,3-propanediol dehydrogenase

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

Reaction

Synonyms

(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-PDDH, 1,3-Pdiol dehydrogenase, 1,3-propanediol dehydrogenase, 1,3-propanediol oxidoreductase, 1,3-propanediol-oxidoreductase, 1,3-propanediol-oxydoreductase, 1,3-propanediol:NAD oxidoreductase, 3-hydroxypropionaldehyde reductase, ADH3, dehydrogenase, 1,3-propanediol, DhaT, lr_0030, lr_1734, NADH-dependent 1,3-PD dehydrogenase, NADH-dependent 1,3-propanediol oxidoreductase, NADH-linked 1,3-propanediol oxidoreductase, PDOR, YqhD

ECTree

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.1 With NAD⁺ or NADP⁺ as acceptor

                1.1.1.202 1,3-propanediol dehydrogenase

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Results	in table
9	Activating Compound
1017	AA Sequence
25	Application
1	CAS Registry Number
35	Cloned(Commentary)
69	Cofactor
6	Crystallization (Commentary)
2	Expression
51	General Information
1	General Stability
21	Inhibitors
19	kcat/KM [mM/s]
1	Ki Value [mM]
54	KM Value [mM]
50	Metals/Ions
37	Molecular Weight [Da]
114	Natural Substrates/ Products (Substrates)
95	Organism
1	Oxidation Stability
4	Pathway
20	PDB ID
37	pH Optimum
7	pH Range
3	pH Stability
2	pI Value
11	Protein Variants
14	Purification (Commentary)
1	Reaction
3	Reaction Type
76	Reference
31	Specific Activity [micromol/min/mg]
225	Substrates and Products (Substrate)
32	Subunits
133	Synonyms
1	Systematic Name
21	Temperature Optimum [°C]
4	Temperature Range [°C]
3	Temperature Stability [°C]
15	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.202 - 1,3-propanediol dehydrogenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

selenomethionine-labeled protein, to 2.4 A resolution. space group P32

Aquifex aeolicus

-

710747

by vapor diffusion in sitting drops at 20°C, 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

Klebsiella pneumoniae

Q7WRJ3

698602

homology modeling with cofactors NADH and NADPH

Klebsiella pneumoniae

Q7WRJ3

712531

purified recombinant His-tagged enzyme, sitting-drop vapour diffusion, 22°C, 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

Klebsiella pneumoniae

-

684171

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+

Oenococcus oeni

A0NIJ1

721395

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

Thermotoga maritima

Q9X022

657320