1.13.11.6: 3-hydroxyanthranilate 3,4-dioxygenase

This is an abbreviated version, for detailed information about 3-hydroxyanthranilate 3,4-dioxygenase, go to the full flat file.

Reaction

3-Hydroxyanthranilate
+
O2
=
2-amino-3-carboxymuconate semialdehyde

Synonyms

3-HAD, 3-HAO, 3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilate oxygenase, 3-hydroxyanthranilic acid oxidase, 3-hydroxyanthranilic acid oxygenase, 3-hydroxyanthranilic oxygenase, 3HAO, EC 1.13.1.6, HAD, oxygenase, 3-hydroxyanthranilate 3,4-di-

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.6 3-hydroxyanthranilate 3,4-dioxygenase

Engineering

Engineering on EC 1.13.11.6 - 3-hydroxyanthranilate 3,4-dioxygenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E110A
-
kcat/Km is 954fold lower than wild-type enzyme
R47A
-
kcat/Km is 7440fold lower than wild-type enzyme. Mutant enzyme shows substrate inhibition
R99A
-
kcat/Km is 22320fold lower than wild-type enzyme
Q105A
-
site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding
R43A
-
site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding
R95A
-
site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding
H52A
inactive enzyme
H93A
24.8% activity of the native enzyme
H96A
inactive enzyme
H52A
-
inactive enzyme
-
H93A
-
24.8% activity of the native enzyme
-
H96A
-
inactive enzyme
-