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Literature summary extracted from

  • Reipa, V.; Holden, M.J.; Vilker, V.L.
    Association and redox properties of the putidaredoxin reductase-nicotinamide adenine dinucleotide complex (2007), Biochemistry, 46, 13235-13244.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.5 expression in Escherichia coli Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.5 Pseudomonas putida P16640
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.5 additional information the midpoint oxidation-reduction potential of PdR is -369 mV at pH 7.6, which is more negative than the pyridine nucleotide NADH/NAD+. The midpoint potential is a hyperbolic function of increasing NAD+ concentration, such that at concentrations of pyridine nucleotide typically found in an intracellular environment, the midpoint potential would be -230 mV, thereby providing the thermodynamically favorable redox equilibria that enables electron transfer from NADH, with thermodynamic control of electron transfer. The PdRox:NAD+ complex is about 5 orders of magnitude weaker than PdRrd:NAD+ binding. These results support a compulsory ordered pathway to describe the electron-transfer processes Pseudomonas putida ?
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Synonyms

EC Number Synonyms Comment Organism
1.18.1.5 Pdr
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 Pseudomonas putida