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Literature summary extracted from

  • Merrill, A.H.; Kazarinoff, M.N.; Tsuge, H.; Horiike, K.; McCormick, D.B.
    Pyridoxamine (pyridoxine) 5-phosphate oxidase from rabbit liver (1979), Methods Enzymol., 62, 568-574.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.4.3.5 bovine serum albumin stabilizes enzyme in dilute solution Oryctolagus cuniculus
1.4.3.5 repeated thawing and refreezing: denaturation Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.5 4-deoxypyridoxine 5'-phosphate
-
 Oryctolagus cuniculus
1.4.3.5 pyridoxal 5'-phosphate
-
 Oryctolagus cuniculus
1.4.3.5 pyridoxal 5'-phosphate oxime
-
 Oryctolagus cuniculus
1.4.3.5 pyridoxaloxime 5'-phosphate
-
 Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.5 27000
-
 2 * 27000, SDS-PAGE Oryctolagus cuniculus

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 in conjugation with pyridoxal kinase the enzyme is responsible for the formation of the coenzyme pyridoxal 5'-phosphate, from the B6 vitamers pyridoxine and pyridoxamine pyridoxal 5'-phosphate + NH3 + H2O2
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.5
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.5 0.41
-
-
 Oryctolagus cuniculus

Storage Stability

EC Number Storage Stability Organism
1.4.3.5 -20°C, 4 years stable, shell-frozen apo- and holoenzyme 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
-
 Oryctolagus cuniculus pyridoxal 5'-phosphate + NH3 + H2O2
-
 ?
1.4.3.5 pyridoxamine 5'-phosphate + H2O + O2 in conjugation with pyridoxal kinase the enzyme is responsible for the formation of the coenzyme pyridoxal 5'-phosphate, from the B6 vitamers pyridoxine and pyridoxamine Oryctolagus cuniculus pyridoxal 5'-phosphate + NH3 + H2O2
-
 ?
1.4.3.5 pyridoxine 5'-phosphate + H2O + O2
-
 Oryctolagus cuniculus pyridoxal 5'-phosphate + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.3.5 dimer 2 * 27000, SDS-PAGE Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.5 FAD bound poorly to apoenzyme Oryctolagus cuniculus
1.4.3.5 FMN binds 1 mol of FMN per mol of dimer Oryctolagus cuniculus
1.4.3.5 FMN analogs modified at position 2, 3, 7, 8, 8alpha and at the ribityl side chain are all bound by the apoenzyme but less tightly than FMN Oryctolagus cuniculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.4.3.5 0.0018
-
 4'-deoxypyridoxine-5'-phosphate
-
 Oryctolagus cuniculus
1.4.3.5 0.002
-
 pyridoxal 5'-phosphate oxime
-
 Oryctolagus cuniculus
1.4.3.5 0.003
-
 pyridoxal 5'-phosphate
-
 Oryctolagus cuniculus