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Literature summary for 1.13.11.6 extracted from

  • Koontz, W.A.; Shiman, R.
    Beef kidney 3-hydroxyanthranilic acid oxygenase. Purification, characterization, and analysis of the assay (1976), J. Biol. Chem., 251, 368-377.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ one Fe2+ per active site Bos taurus
Fe3+ does not seem to bind to the enzyme Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
gel filtration, readily aggregates to form inactive higher molecular weight oligomers Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
140
-
-
Bos taurus

Storage Stability

Storage Stability Organism
-90°C, frozen in dry ice-ethanol bath, partially purified enzyme is stable for at least 1 month, purified enzyme is unstable Bos taurus
0°C, 0.01 M collidine chloride, 0.01 M potassium chloride, pH 6.5, about 15% loss of activity after 1 month, purified enzyme Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxyanthranilate + O2
-
Bos taurus 2-amino-3-carboxymuconate semialdehyde
-
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