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Literature summary for 1.4.3.5 extracted from

  • di Salvo, M.L.; Safo, M.K.; Musayev, F.N.; Bossa, F.; Schirch, V.
    Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate oxidase (2003), Biochim. Biophys. Acta, 1647, 76-82.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structures are defined at 2.0-2.1 A resolution Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information pyridoxamine 5'-phosphate shows no substrate inhibition Escherichia coli
pyridoxal 5'-phosphate
-
Escherichia coli
pyridoxine 5'-phosphate substrate inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information KM-values of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M Escherichia coli
0.002
-
pyridoxine 5'-phosphate pH 8.5, 37°C Escherichia coli
0.105
-
pyridoxamine 5'-phosphate
-
Escherichia coli
0.18
-
O2
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyridoxamine 5'-phosphate + H2O + O2 Escherichia coli terminal step in de novo biosynthesis of pyridoxal 5'-phosphate pyridoxal 5'-phosphate + NH3 + H2O2
-
?
pyridoxine 5'-phosphate + H2O + O2 Escherichia coli terminal step in de novo biosynthesis of pyridoxal 5'-phosphate pyridoxal 5'-phosphate + H2O2
-
?

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 terminal step in de novo biosynthesis of pyridoxal 5'-phosphate Escherichia coli pyridoxal 5'-phosphate + NH3 + H2O2
-
?
pyridoxamine 5'-phosphate + H2O + O2 the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate Escherichia coli pyridoxal 5'-phosphate + NH3 + H2O2
-
?
pyridoxine 5'-phosphate + H2O + O2 terminal step in de novo biosynthesis of pyridoxal 5'-phosphate Escherichia coli pyridoxal 5'-phosphate + H2O2
-
?
pyridoxine 5'-phosphate + H2O + O2 the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate Escherichia coli pyridoxal 5'-phosphate + H2O2
-
?

Synonyms

Synonyms Comment Organism
PNPOx
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information turnover numbers of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M Escherichia coli
0.13
-
pyridoxine 5'-phosphate pH 8.5, 37°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FMN two molecules of FMN are noncovalently bound to the dimeric form of oxidase Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.008
-
pyridoxal 5'-phosphate
-
Escherichia coli
0.05
-
pyridoxine 5'-phosphate substrate inhibition Escherichia coli