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Literature summary extracted from

  • Howe, G.W.; van der Donk, W.A.
    Temperature-independent kinetic isotope effects as evidence for a Marcus-like model of hydride tunneling in phosphite dehydrogenase (2019), Biochemistry, 58, 4260-4268.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.20.1.1 gene ptxD, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3) Stutzerimonas stutzeri

Protein Variants

EC Number Protein Variants Comment Organism
1.20.1.1 T104A site-directed mutagenesis, the mutation has only a modest impact on the derived kinetic parameters compared to wild-type enzyme Stutzerimonas stutzeri
1.20.1.1 T104G site-directed mutagenesis, the mutation has only a modest impact on the derived kinetic parameters compared to wild-type enzyme Stutzerimonas stutzeri
1.20.1.1 T104S site-directed mutagenesis, the mutation has only a modest impact on the derived kinetic parameters compared to wild-type enzyme Stutzerimonas stutzeri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.20.1.1 additional information
-
 additional information pre-steady-state and steady-state kinetic analysis of wild-type and mutant enzymes, overview. The hydride transfer remains entirely rate-limiting between 5°C and 45°C Stutzerimonas stutzeri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.20.1.1 phosphonate + NAD+ + H2O Stutzerimonas stutzeri
-
 phosphate + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.20.1.1 Stutzerimonas stutzeri O69054 Stutzerimonas stutzeri
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.20.1.1 recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and desalting gel filtration Stutzerimonas stutzeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.20.1.1 additional information phosphite dehydrogenase catalyzes the transfer of a hydride from phosphite to NAD+, producing phosphate and NADH. Temperature-independent kinetic isotope effects show evidence for a Marcus-like model of hydride tunneling in phosphite dehydrogenase. The hydride transfer remains entirely rate-limiting between 5°C and 45°C Stutzerimonas stutzeri ?
-
 ?
1.20.1.1 phosphonate + NAD+ + H2O
-
 Stutzerimonas stutzeri phosphate + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.20.1.1 17X-PTDH
-
 Stutzerimonas stutzeri
1.20.1.1 phosphite dehydrogenase
-
 Stutzerimonas stutzeri
1.20.1.1 PTDH
-
 Stutzerimonas stutzeri
1.20.1.1 PtxD
-
 Stutzerimonas stutzeri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.20.1.1 25
-
 assay at Stutzerimonas stutzeri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.20.1.1 7.2 7.3 assay at Stutzerimonas stutzeri

Cofactor

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