1.13.11.50: acetylacetone-cleaving enzyme

This is an abbreviated version, for detailed information about acetylacetone-cleaving enzyme, go to the full flat file.

Reaction

Pentane-2,4-dione
+
O2
=
acetate
+
methylglyoxal

Synonyms

acetylacetone dioxygenase, acetylacetone-cleaving enzyme, b-diketone dioxygenase, cupin-type dioxygenase, diketone cleaving dioxygenase, diketone cleaving enzyme, diketone dioxygenase, diketone-cleaving dioxygenase, diketone-cleaving enzyme, Dke1, oxygenase, b-diketone di-, pentane-2,4-dione hydrolase

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
                1.13.11.50 acetylacetone-cleaving enzyme

Engineering

Engineering on EC 1.13.11.50 - acetylacetone-cleaving enzyme

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E69Q
-
lower thermal stability of beta-sheet secondary structure, half catalytic center activity and remarkably silent difference in apparent substrate binding compared to the wild type enzyme
E98A
-
site-direted mutagenesis
F115A
-
site-directed mutagenesis, the mutant shows reduced turnover and altered iron binding compared to the wild-type enzyme
F119A
-
site-directed mutagenesis, the mutant shows reduced turnover and altered iron binding compared to the wild-type enzyme
F59A
-
site-directed mutagenesis, the mutant shows reduced turnover and altered iron binding compared to the wild-type enzyme
H104E
-
no activity in initial rate assays with substrate pentan-2,4-dione, no binding of Fe2+ at binding site I, small effect on other metal ions
H104N
-
approximately 1% of the specific activity of wild-type enzyme with substrate pentan-2,4-dione, retains binding affinity for Fe2+ at binding site I, binding seems to be tighter than in wild-type, small effect on other metal ions
H62E
-
no activity in initial rate assays with substrate pentan-2,4-dione, no binding of Fe2+ at binding site I, small effect on other metal ions
H62N
-
no activity in initial rate assays with substrate pentan-2,4-dione, no binding of Fe2+ at binding site I, binding disruption of Cu2+, Mn2+, and Ni2+ compared with wild-type
H64D
-
no activity in initial rate assays with substrate pentan-2,4-dione, no binding of Fe2+ at binding site I, small effect on other metal ions
H64E
-
no activity in initial rate assays with substrate pentan-2,4-dione, no binding of Fe2+ at binding site I, small effect on other metal ions
H64N
-
conversion of substrate in a strictly Fe2+-concentration dependent manner, substrate pentan-2,4-dione, no binding of Fe2+ at binding site I, small effect on other metal ions
R80A/E98A
-
site-direted mutagenesis
T107A
-
site-direted mutagenesis
Y70A/R80A/E98A
-
site-direted mutagenesis
Y70F/R80A/E98A
-
site-direted mutagenesis
additional information
-
the exchange of 3 histidines in the Fe2+-binding centre shows that these histidines are crucial for for binding Fe2+ and for Fe2+-dependent dioxygenase activity