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Literature summary extracted from

  • Di Salvo, M.L.; Ko, T.P.; Musayev, F.N.; Raboni, S.; Schirch, V.; Safo, M.K.
    Active site structure and stereospecificity of Escherichia coli pyridoxine-5'-phosphate oxidase (2002), J. Mol. Biol., 315, 385-397.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.5 wild-type and mutant enzyme Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.3.5 enzyme in complex with pyridoxal 5'-phosphate, space group C2, 2.07 A resolution Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.5 D49A decrease in affinity for pyridoxine 5'-phosphate Escherichia coli
1.4.3.5 H199A decrease in affinity for pyridoxine 5'-phosphate Escherichia coli
1.4.3.5 H199N little decrease in pyridoxine 5'-phosphate turnover Escherichia coli
1.4.3.5 R14E decrease in affinity for pyridoxine 5'-phosphate Escherichia coli
1.4.3.5 R14M decrease in affinity for pyridoxine 5'-phosphate Escherichia coli
1.4.3.5 R197E strong decrease in affinity for pyridoxine 5'-phosphate Escherichia coli
1.4.3.5 R197M catalyzes removal of the proS hydrogen atom from (4'R)-3H-pyridoxamine 5'-phosphate, decrease in affinity for pyridoxine 5'-phosphate Escherichia coli
1.4.3.5 Y17F decrease in affinity for pyridoxine 5'-phosphate Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.5 0.0003
-
 pyridoxine 5'-phosphate
-
 Escherichia coli
1.4.3.5 0.0003
-
 pyridoxine 5'-phosphate H199N mutant enzyme Escherichia coli
1.4.3.5 0.001
-
 pyridoxine 5'-phosphate D49A and Y17F mutant enzyme Escherichia coli
1.4.3.5 0.002
-
 pyridoxine 5'-phosphate R14E mutant enzyme Escherichia coli
1.4.3.5 0.0026
-
 pyridoxine 5'-phosphate R14M mutant enzyme Escherichia coli
1.4.3.5 0.07
-
 pyridoxine 5'-phosphate H199A mutant enzyme Escherichia coli
1.4.3.5 0.09
-
 pyridoxine 5'-phosphate R197M mutant enzyme Escherichia coli
1.4.3.5 2.4
-
 pyridoxine 5'-phosphate R197M mutant enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.5 Escherichia coli P0AFI7
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.4.3.5 pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2 enzyme is specific for removal of the pro-R hydrogen atom from the prochiral C4' carbon atom of pyridoxamine 5'-phosphate, hydride ion mechanism is suggested Escherichia coli
a

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.5 0.008
-
 pyridoxine 5'-phosphate R197M mutant enzyme Escherichia coli
1.4.3.5 0.03
-
 pyridoxine 5'-phosphate H199N mutant enzyme Escherichia coli
1.4.3.5 0.03
-
 pyridoxine 5'-phosphate R197M mutant enzyme Escherichia coli
1.4.3.5 0.06
-
 pyridoxine 5'-phosphate D49A mutant enzyme Escherichia coli
1.4.3.5 0.13
-
 pyridoxine 5'-phosphate
-
 Escherichia coli
1.4.3.5 0.14
-
 pyridoxine 5'-phosphate H199A mutant enzyme Escherichia coli
1.4.3.5 0.14
-
 pyridoxine 5'-phosphate R14M mutant enzyme Escherichia coli
1.4.3.5 0.16
-
 pyridoxine 5'-phosphate R14E mutant enzyme Escherichia coli
1.4.3.5 0.6
-
 pyridoxine 5'-phosphate Y17F mutant enzyme Escherichia coli