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.
Word Map on EC 1.13.11.50
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1.13.11.50
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facial
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acinetobacter
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johnsonii
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nonheme
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methylglyoxal
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five-coordinate
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o2-dependent
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fe2+-dependent
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dioxygen-dependent
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six-coordinate
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bidentate
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uv-vis
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ferrous
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non-native
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r-groups
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enzyme-bound
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enol
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metal-binding
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2-his-1-carboxylate
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ironii
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high-spin
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environmental protection
- 1.13.11.50
-
facial
- acinetobacter
- johnsonii
-
nonheme
- methylglyoxal
-
five-coordinate
-
o2-dependent
-
fe2+-dependent
-
dioxygen-dependent
-
six-coordinate
-
bidentate
-
uv-vis
-
ferrous
-
non-native
-
r-groups
-
enzyme-bound
-
enol
-
metal-binding
-
2-his-1-carboxylate
-
ironii
-
high-spin
- environmental protection
Reaction
Synonyms
acetylacetone dioxygenase, acetylacetone-cleaving enzyme, b-diketone dioxygenase, beta-diketone dioxygenase, cupin-type dioxygenase, diketone cleaving dioxygenase, diketone cleaving enzyme, diketone dioxygenase, diketone-cleaving dioxygenase, diketone-cleaving enzyme, DKDO, Dke1, oxygenase, b-diketone di-, pentane-2,4-dione hydrolase
ECTree
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Engineering
Engineering on EC 1.13.11.50 - acetylacetone-cleaving enzyme
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E69Q
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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
E98Q
F115A
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site-directed mutagenesis, the mutant shows reduced turnover and altered iron binding compared to the wild-type enzyme
F119A
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site-directed mutagenesis, the mutant shows reduced turnover and altered iron binding compared to the wild-type enzyme
F59A
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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
Y70A
Y70F
additional information
E98Q
an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein
R80A
mutation causes relocation of Glu11 from neighbor subunit closer to His104, enabling formation of the Glu11(OE1/2)-His104(NE2H/CD2H) H-bond
Y70A
an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein
Y70F
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site-directed mutagenesis, the mutant shows reduced turnover and altered iron binding compared to the wild-type enzyme
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
additional information
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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