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Literature summary for 1.13.11.6 extracted from

  • Serrano, A.E.; Nagayama, F.
    Liver 3-hydroxyanthranilic acid oxygenase activity in rainbow trout (Oncorhynchus mykiss) (1991), Comp. Biochem. Physiol. B, 99, 275-280.
    View publication on PubMed

General Stability

General Stability Organism
stability of enzyme in crude extract Oncorhynchus mykiss
thawing and refreezing: crude enzyme extract at 20°C, relatively stable in presence of Fe2+, about 30% loss of activity after 2 thawings Oncorhynchus mykiss

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Oncorhynchus mykiss

Organism

Organism UniProt Comment Textmining
Oncorhynchus mykiss
-
rainbow trout
-

Purification (Commentary)

Purification (Comment) Organism
-
Oncorhynchus mykiss

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Oncorhynchus mykiss
-

Storage Stability

Storage Stability Organism
0°C, 66.7 mM Tris-HCl buffer, pH 8.0, 90 min, approximately 25% loss of activity Oncorhynchus mykiss
25°C, 66.7 mM Tris-HCl buffer, pH 8.0, 90 min, approximately 70% loss of activity Oncorhynchus mykiss

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxyanthranilate + O2
-
Oncorhynchus mykiss 2-amino-3-carboxymuconate semialdehyde
-
?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
-
50 enzyme activity increased almost linearly with temperature, beyond a sharp drop Oncorhynchus mykiss

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
determination on heat-reactivated extracts after inactivation Oncorhynchus mykiss

pH Range

pH Minimum pH Maximum Comment Organism
5 7.5 determination on heat-reactivated extracts after inactivation Oncorhynchus mykiss

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.5
-
most stable, above extremly unstable Oncorhynchus mykiss