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
-
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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Inhibitors
Inhibitors on EC 1.13.11.50 - acetylacetone-cleaving enzyme
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Cu2+
20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate
hexacyanoferrate(III)
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2.5 mM, 80% decrease in activity within 10 min
Mn2+
20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate
Ni2+
20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate
Zn2+
20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate
H2O2
1 M H2O2 causes complete loss of enzyme activity in less than 10 min, contains no Fe2+ (probably oxidized to Fe3+), partial reconstitution (40%) with 2 mM Fe2+, 20 mM Tris/HCl buffer, pH 7.5, 25°C