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Literature summary for 1.4.3.5 extracted from

  • Barile, A.; Battista, T.; Fiorillo, A.; di Salvo, M.; Malatesta, F.; Tramonti, A.; Ilari, A.; Contestabile, R.
    Identification and characterization of the pyridoxal 5-phosphate allosteric site in Escherichia coli pyridoxine 5-phosphate oxidase (2021), J. Biol. Chem., 296, 100795 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.5

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
K145A/F177A the Tm-value is about 1°C higher than the Tm-value of the wild-type enzyme Escherichia coli
N84A/K145A/F177A the Tm-value is about 3.3°C lower than the Tm-value of the wild-type enzyme Escherichia coli
N84W/K145A/F177A the Tm-value is about 3.4°C lower than the Tm-value of the wild-type enzyme Escherichia coli
R215L the Tm-value is 1°C lower than the Tm-value of the wild-type enzyme Escherichia coli
R23L the Tm-value is identical to the Tm-value of the wild-type enzyme Escherichia coli
R23L/R215L loosening of the allosteric coupling Escherichia coli
R23L/R24L loosening of the allosteric coupling Escherichia coli
R23L/R24L/R21L complete loss of allosteric properties. The Tm-value is about 2°C lower than the Tm-value of the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
pyridoxal 5'-phosphate the enzyme undergoes an allosteric feedback inhibition by pyridoxal 5'-phosphate (PLP) caused by a strong allosteric coupling between PLP binding at the allosteric site and substrate binding at the active site. One PLP molecule is bound at the allosteric site of one monomer Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0016
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, wild-type enzyme Escherichia coli
0.0017
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R23L Escherichia coli
0.0021
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R23L/R24L Escherichia coli
0.0024
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme K145A/F177A Escherichia coli
0.0026
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R215L Escherichia coli
0.0031
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme N84W/K145A/F177A Escherichia coli
0.0032
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme N84A/K145A/F177A Escherichia coli
0.0032
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R23L/R215L Escherichia coli
0.0034
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R23L/R24L/R215L Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyridoxine 5'-phosphate + O2 Escherichia coli
-
 pyridoxal 5'-phosphate + H2O2
-
 ?
pyridoxine 5'-phosphate + O2 Escherichia coli K12
-
 pyridoxal 5'-phosphate + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFI7
-
-
Escherichia coli K12 P0AFI7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyridoxine 5'-phosphate + O2
-
 Escherichia coli pyridoxal 5'-phosphate + H2O2
-
 ?
pyridoxine 5'-phosphate + O2
-
 Escherichia coli K12 pyridoxal 5'-phosphate + H2O2
-
 ?

Subunits

Subunits Comment Organism
homodimer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
PdxH
-
 Escherichia coli
PNPO
-
 Escherichia coli
pyridoxine 5'-phosphate oxidase
-
 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
66.6
-
 Tm-value, mutant enzyme N84W/K145A/F177A Escherichia coli
66.7
-
 Tm-value, mutant enzyme N84A/K145A/F177A Escherichia coli
68
-
 Tm-value, mutant enzyme R23L/R24L/R215L Escherichia coli
68.9
-
 Tm-value, mutant enzyme R23L/R215L Escherichia coli
69
-
 Tm-value, mutant enzyme R215L Escherichia coli
70
-
 Tm-value, wild-type enzyme Escherichia coli
70
-
 Tm-value, mutant enzyme R23L Escherichia coli
70.9
-
 Tm-value, mutant enzyme K145A/F177A Escherichia coli
71.1
-
 Tm-value, mutant enzyme R23L/R24L Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme N84W/K145A/F177A Escherichia coli
0.05
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R215L Escherichia coli
0.05
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R23L/R215L Escherichia coli
0.07
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme N84A/K145A/F177A Escherichia coli
0.09
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R23L Escherichia coli
0.09
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R23L/R24L/R215L Escherichia coli
0.17
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme K145A/F177A Escherichia coli
0.19
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, mutant enzyme R23L-R24L Escherichia coli
0.25
-
 pyridoxine 5'-phosphate pH 7.6, 37°C, wild-type enzyme Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FMN FMN-dependent enzyme Escherichia coli

General Information

General Information Comment Organism
metabolism the enzyme is responsible for the last step of pyridoxal 5'-phosphate biosynthesis and is also involved in the pyridoxal 5'-phosphate salvage pathway Escherichia coli