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Literature summary extracted from

  • Buckthal, D.J.; Roche, P.A.; Moorehead, T.J.; Forbes, B.J.R.; Hamilton, G.A.
    4-Hydroxyphenylpyruvate dioxygenase from pig liver (1987), Methods Enzymol., 142, 132-138.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.13.11.27 long-term storage of concentrated solutions in presence of air leads to polymerization Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.27 additional information
-
additional information the Km-value is the same at 25°C and at 38°C Sus scrofa
1.13.11.27 0.04
-
4-hydroxyphenylpyruvate
-
Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.27 copper 0.4 atoms of Fe per 89000 Da enzyme. Removal of copper does not correlate with loss of activity Sus scrofa
1.13.11.27 Iron 0.9 atoms of Fe per 89000 Da enzyme. Removal of iron correlates with loss of activity Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.27 44000
-
2 * 44000, nonidentical subunits, SDS-PAGE Sus scrofa
1.13.11.27 89000
-
method not mentioned Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.27 4-hydroxyphenylpyruvate + O2 Sus scrofa enzyme participates in catabolism of tyrosine homogentisate + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.27 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.27
-
Sus scrofa

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.27 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2 rate-determining step in catalysis is a protein conformation change Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.13.11.27 liver
-
Sus scrofa
-

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 51
-
-
Sus scrofa

Storage Stability

EC Number Storage Stability Organism
1.13.11.27 -20°C, concentrated enzyme solution, 1.0 mg/ml, stable for 6 months or more Sus scrofa
1.13.11.27 4°C, 10 mM sodium acetate buffer, pH 6.0, little loss of activity after 2 months Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.27 4-hydroxyphenylpyruvate + O2 best substrate Sus scrofa homogentisate + CO2
-
?
1.13.11.27 4-hydroxyphenylpyruvate + O2 enzyme participates in catabolism of tyrosine Sus scrofa homogentisate + CO2
-
?
1.13.11.27 phenylpyruvate + O2 at 10% of the activity with 4-hydroxyphenylpyruvate Sus scrofa 2-hydroxyphenylacetate + CO2
-
?

Subunits

EC Number Subunits Comment Organism
1.13.11.27 dimer 2 * 44000, nonidentical subunits, SDS-PAGE Sus scrofa

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.13.11.27 additional information
-
enzymatic rate increases approximately 5fold for every 10°C increase, Km-value is the same at 25°C and at 38°C Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.13.11.27 5 7 reaction rate is constant between pH 5 and pH 7 Sus scrofa