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Literature summary for 1.4.3.5 extracted from

  • Choi, J.D.; Bowers-Komro, M.; Davis, M.D.; Edmondson, D.E.; McCormick, D.B.
    Kinetic properties of pyridoxamine (pyridoxine)-5-phosphate oxidase from rabbit liver (1983), J. Biol. Chem., 258, 840-845.
    View publication on PubMed
Search for more literature for 1.4.3.5

Inhibitors

Inhibitors Comment Organism Structure
additional information no substrate inhibition with pyridoxamine 5'-phosphate Oryctolagus cuniculus
pyridoxine 5'-phosphate substrate inhibition Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0036
-
 pyridoxamine 5'-phosphate
-
 Oryctolagus cuniculus
0.0082
-
 pyridoxine 5'-phosphate
-
 Oryctolagus cuniculus
0.085
-
 O2 cosubstrate pyridoxamine 5'-phosphate Oryctolagus cuniculus
0.182
-
 O2 cosubstrate pyridoxine 5'-phosphate Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2 kinetic mechanims via either a binary or a ternary complex mechanism, depending on nature of substrate, ternary complex mechanism with pyridoxamine 5'-phosphate Oryctolagus cuniculus
a

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.103
-
 pyridoxamine 5'-phosphate
-
 Oryctolagus cuniculus
0.7
-
 pyridoxine 5'-phosphate
-
 Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.05
-
 pyridoxine 5'-phosphate
-
 Oryctolagus cuniculus