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Literature summary for 1.4.3.5 extracted from

  • Notheis, C.; Drewke, C.; Leistner, E.
    Purification and characterization of the pyridoxol-5'-phosphate:oxygen oxidoreductase (deaminating) from Escherichia coli (1995), Biochim. Biophys. Acta, 1247, 265-271.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli as maltose binding protein fusion Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
pyridoxal 5'-phosphate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.368
-
pyridoxal 5'-phosphate recombinant enzyme after cleavage from fusion protein Escherichia coli
0.4
-
pyridoxamine 5'-phosphate recombinant enzyme after cleavage from fusion protein Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25500
-
recombinant enzyme after cleavage from fusion protein Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyridoxamine 5'-phosphate + H2O + O2
-
Escherichia coli pyridoxal 5'-phosphate + NH3 + H2O2
-
?

Subunits

Subunits Comment Organism
monomer 1 * 25500, recombinant enzyme after cleavage from fusion protein, gel filtration Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
28
-
pyridoxamine 5'-phosphate recombinant enzyme after cleavage from fusion protein Escherichia coli
33
-
pyridoxal 5'-phosphate recombinant enzyme after cleavage from fusion protein Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
recombinant enzyme after cleavage from fusion protein Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.008
-
pyridoxal 5'-phosphate
-
Escherichia coli