1.13.11.48: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

This is an abbreviated version!
For detailed information about 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase, go to the full flat file.

Reaction

3-hydroxy-2-methyl-1H-quinolin-4-one
+
O2
=
N-acetylanthranilate
+
CO

Synonyms

1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase, 1H-3-hydroxy-4-oxoquinaldine oxygenase, 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase, HOD, HodC, More

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
                1.13.11.48 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

Temperature Stability

Temperature Stability on EC 1.13.11.48 - 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
enzyme in native reduced state (40 mM dithiothreitol) of mutant enzyme, 10 mM sodium phosphate and 10 mM sodium borate buffer, pH 7.5, unfolding starts at 40°C
10 - 50
native oxidized state of mutant enzyme, 10 mM sodium phosphate and 10 mM sodium borate buffer, pH 7.5, unfolding starts at 50°C
additional information
-
recombinant His6HodC exhibits three-state unfolding with an intermediate state I that exhibits at the transition temperature a volume larger than that of the native or denatured state. The intermediate state I is also associated with the highest isothermal expansion coefficient, alphaP, of the three states and exhibits a significantly lower percentage of R-helical structure than the native state. The stability difference between the native and intermediate state is rather small which makes I a potential candidate for reactions with various ligands, particularly those having a preference for the apparently preserved beta-type motifs