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Literature summary for 1.4.3.5 extracted from

  • Gu, J.; Chen, Y.; Guo, H.; Sun, M.; Yang, M.; Wang, X.; Zhang, X.; Deng, J.
    Lysine acetylation regulates the activity of Escherichia coli pyridoxine 5'-phosphate oxidase (2017), Acta Biochim. Biophys. Sin., 49, 186-192 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
K159Q the mutation has no effect on the catalytic activity Escherichia coli
K159R the mutation has no effect on the catalytic activity Escherichia coli
K72A the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme Escherichia coli
K72P the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme Escherichia coli
K72Q the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme Escherichia coli
K72R the mutant shows a slight decrease of the catalytic activity compared to the wild type enzyme Escherichia coli

General Stability

General Stability Organism
acetylation leads to a decrease of the enzymatic activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.037
-
pyridoxine 5'-phosphate wild type enzyme, at pH 8.0 and 37°C Escherichia coli
0.113
-
pyridoxine 5'-phosphate mutant enzyme K72P, at pH 8.0 and 37°C Escherichia coli
0.219
-
pyridoxine 5'-phosphate mutant enzyme K72R, at pH 8.0 and 37°C Escherichia coli
0.625
-
pyridoxine 5'-phosphate mutant enzyme K72A, at pH 8.0 and 37°C Escherichia coli
0.946
-
pyridoxine 5'-phosphate mutant enzyme K72Q, at pH 8.0 and 37°C 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
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel affinity column chromatography 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
-
?

Subunits

Subunits Comment Organism
homodimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
PNPOx
-
Escherichia coli
pyridoxine 5'-phosphate oxidase
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0002
-
pyridoxine 5'-phosphate mutant enzyme K72P, at pH 8.0 and 37°C Escherichia coli
0.0004
-
pyridoxine 5'-phosphate mutant enzyme K72A, at pH 8.0 and 37°C Escherichia coli
0.0015
-
pyridoxine 5'-phosphate mutant enzyme K72Q, at pH 8.0 and 37°C Escherichia coli
0.022
-
pyridoxine 5'-phosphate wild type enzyme, at pH 8.0 and 37°C Escherichia coli
0.024
-
pyridoxine 5'-phosphate mutant enzyme K72R, at pH 8.0 and 37°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FMN
-
Escherichia coli