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Literature summary extracted from

  • Johnson-Winters, K.; Purpero, V.M.; Kavana, M.; Nelson, T.; Moran, G.R.
    (4-Hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis: the basis for ordered substrate addition (2003), Biochemistry, 42, 2072-2080.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.27 0.027
-
 (4-hydroxyphenyl)-pyruvate pH 7.0, 25°C Streptomyces avermitilis
1.13.11.27 0.069
-
 O2 pH 7.0, 25°C Streptomyces avermitilis

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.27 Streptomyces avermitilis
-
 expression in Escherichia coli
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.27
-
 Streptomyces avermitilis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.27 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 addition of substrate and oxygen to the holoenzyme is formally random, holo-enzym in complex with substrate has a 3600-fold increase in oxygen reactivity Streptomyces avermitilis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.11.27 10.6
-
 pH 7.0, 25°C Streptomyces avermitilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.27 (4-hydroxyphenyl)-pyruvate + O2
-
 Streptomyces avermitilis homogentisate + CO2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.27 6.8
-
 (4-hydroxyphenyl)-pyruvate
-
 Streptomyces avermitilis