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Literature summary extracted from

  • Fogle, E.J.; van der Donk, W.A.
    Pre-steady-state studies of phosphite dehydrogenase demonstrate that hydride transfer is fully rate limiting (2007), Biochemistry, 46, 13101-13108.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.20.1.1 additional information has great potential for cofactor regeneration Stutzerimonas stutzeri

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.20.1.1 His6-tagged PTDH overexpressed in Escherichia coli BL21(DE3) harboring a pET15b vector Stutzerimonas stutzeri

Protein Variants

EC Number Protein Variants Comment Organism
1.20.1.1 D79A significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates Stutzerimonas stutzeri
1.20.1.1 D79N has kinetic parameters more similar to those of wild-type Stutzerimonas stutzeri
1.20.1.1 E266Q higher activity, steady-state and pre-steady-state rates are comparable Stutzerimonas stutzeri
1.20.1.1 K76A pre-steady-state rates are approximately the same as the steady-state rates Stutzerimonas stutzeri
1.20.1.1 additional information thermostable mutant 12X-PTDH with higher solubility than the wild-type. Thermostable mutant with dual cofactor specificity NADP-12X NAD shows pre-steady-state behavior very similar to that observed with 12X-PTDH and the wild-type enzyme. Pre-steady-state traces of thermostable mutant with dual cofactor specificity NADP-12X NADP shows curvature with NADP, particularly with protiated phosphite Stutzerimonas stutzeri
1.20.1.1 R237K low activity, absence of a significant burst in the pre-steady-state Stutzerimonas stutzeri

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.20.1.1 additional information slow steps after hydride transfer do not significantly limit the rate of reaction for the wild-type enzyme, the active site mutants, or the thermostable mutant Stutzerimonas stutzeri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.20.1.1 0.001
-
 phosphite mutant R237K Stutzerimonas stutzeri
1.20.1.1 0.012
-
 NAD+ mutant D79N Stutzerimonas stutzeri
1.20.1.1 0.035
-
 phosphite mutant D79N Stutzerimonas stutzeri
1.20.1.1 0.035
-
 NAD+ wild-type Stutzerimonas stutzeri
1.20.1.1 0.055
-
 phosphite wild-type Stutzerimonas stutzeri
1.20.1.1 0.062
-
 NAD+ mutant D79A Stutzerimonas stutzeri
1.20.1.1 1
-
 NAD+ mutant R237K Stutzerimonas stutzeri
1.20.1.1 1.2
-
 phosphite mutant D79A Stutzerimonas stutzeri

Organism

EC Number Organism UniProt Comment Textmining
1.20.1.1 Stutzerimonas stutzeri
-
-
-
1.20.1.1 Stutzerimonas stutzeri WW88
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.20.1.1 on Ni2+ affinity resin Stutzerimonas stutzeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.20.1.1 phosphite + H2O + NAD+ Asp79 is important in orienting Arg237 for proper interaction with phosphite Stutzerimonas stutzeri phosphate + NADH + H+
-
 ?
1.20.1.1 phosphite + H2O + NAD+ Asp79 is important in orienting Arg237 for proper interaction with phosphite Stutzerimonas stutzeri WW88 phosphate + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.20.1.1 phosphite dehydrogenase
-
 Stutzerimonas stutzeri
1.20.1.1 PTDH
-
 Stutzerimonas stutzeri

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.20.1.1 0.0126
-
 phosphite mutant R237K Stutzerimonas stutzeri
1.20.1.1 0.0305
-
 phosphite mutant D79A Stutzerimonas stutzeri
1.20.1.1 0.23
-
 phosphite mutant D79N Stutzerimonas stutzeri
1.20.1.1 0.58
-
 phosphite mutant NADP-12X NAD Stutzerimonas stutzeri
1.20.1.1 0.621
-
 phosphite mutant K76A Stutzerimonas stutzeri
1.20.1.1 2.04
-
 phosphite mutant NADP-12X NAD Stutzerimonas stutzeri
1.20.1.1 2.42
-
 phosphite wild-type Stutzerimonas stutzeri
1.20.1.1 3.26
-
 phosphite thermostable mutant 12X-PTDH Stutzerimonas stutzeri
1.20.1.1 7.5
-
 phosphite mutant E266Q Stutzerimonas stutzeri

Cofactor

EC Number Cofactor Comment Organism Structure
1.20.1.1 NAD(P)+
-
 Stutzerimonas stutzeri