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Literature summary extracted from

  • Merrill, A.H.; Horiike, K.; McCormick, D.B.
    Evidence for the regulation of pyridoxal 5-phosphate formation in liver by pyridoxamine (pyridoxine) 5 -phosphate oxidase (1978), Biochem. Biophys. Res. Commun., 83, 984-990.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.5 pyridoxal 5'-phosphate competitive inhibition; competitive product inhibition, overview Oryctolagus cuniculus
1.4.3.5 pyridoxal 5'-phosphate competitive inhibition Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.5 0.004
-
pyridoxine 5'-phosphate enzyme activity in liver homogenate Rattus norvegicus
1.4.3.5 0.008
-
pyridoxamine 5'-phosphate enzyme activity in liver homogenate Rattus norvegicus
1.4.3.5 0.011
-
pyridoxamine 5'-phosphate enzyme activity in liver homogenate Oryctolagus cuniculus
1.4.3.5 0.015
-
pyridoxamine 5'-phosphate enzyme activity in cytosol Oryctolagus cuniculus
1.4.3.5 0.016
-
pyridoxine 5'-phosphate pure enzyme in 200 mM potassium phosphate pH 7.0 Oryctolagus cuniculus
1.4.3.5 0.016
-
pyridoxine 5'-phosphate pH 7.0, 37°C Oryctolagus cuniculus
1.4.3.5 0.017
-
pyridoxine 5'-phosphate enzyme activity in cytosol Oryctolagus cuniculus
1.4.3.5 0.017
-
pyridoxine 5'-phosphate enzyme activity in liver homogenate Oryctolagus cuniculus
1.4.3.5 0.018
-
pyridoxamine 5'-phosphate pH 8.0, 37°C Oryctolagus cuniculus
1.4.3.5 0.022
-
pyridoxine 5'-phosphate enzyme activity in liver homogenate in the presence of 0.005 mM pyridoxal 5'-phosphate Rattus norvegicus
1.4.3.5 0.024
-
pyridoxamine 5'-phosphate pure enzyme in 200 mM potassium phosphate pH 7.0 Oryctolagus cuniculus
1.4.3.5 0.024
-
pyridoxamine 5'-phosphate pH 7.0, 37°C Oryctolagus cuniculus
1.4.3.5 0.025
-
pyridoxine 5'-phosphate pH 8.0, 37°C Oryctolagus cuniculus
1.4.3.5 0.039
-
pyridoxamine 5'-phosphate enzyme activity in liver homogenate in the presence of 0.005 mM pyridoxal 5'-phosphate Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.3.5 pyridoxamine 5'-phosphate + H2O + O2 Oryctolagus cuniculus
-
pyridoxal 5'-phosphate + NH3 + H2O2
-
?
1.4.3.5 pyridoxine 5'-phosphate + O2 Oryctolagus cuniculus
-
pyridoxal 5'-phosphate + H2O2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.5 Oryctolagus cuniculus
-
-
-
1.4.3.5 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.5 native enzyme from liver Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.5 liver
-
Rattus norvegicus
-
1.4.3.5 liver
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.5 pyridoxamine 5'-phosphate + H2O + O2
-
Rattus norvegicus pyridoxal 5'-phosphate + NH3 + H2O2
-
?
1.4.3.5 pyridoxamine 5'-phosphate + H2O + O2
-
Oryctolagus cuniculus pyridoxal 5'-phosphate + NH3 + H2O2
-
?
1.4.3.5 pyridoxine 5'-phosphate + FMN
-
Rattus norvegicus pyridoxal 5'-phosphate + FMNH2
-
?
1.4.3.5 pyridoxine 5'-phosphate + O2
-
Oryctolagus cuniculus pyridoxal 5'-phosphate + H2O2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.4.3.5 pyridoxamine (pyridoxine) 5'-phosphate oxidase
-
Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.5 37
-
assay at Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.5 7 8 assay at Oryctolagus cuniculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.4.3.5 0.003
-
pyridoxal 5'-phosphate pure enzyme in 200 mM potassium phosphate pH 7.0 or enzyme activity in liver homogenate, substrate pyridoxamine 5' phosphate or pyridoxine 5'-phosphate Oryctolagus cuniculus
1.4.3.5 0.003
-
pyridoxal 5'-phosphate pH 8.0, 37°C Oryctolagus cuniculus