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
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Substrates Products
Substrates Products on EC 1.13.11.50 - acetylacetone-cleaving enzyme
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REACTION DIAGRAM
acetate + 2-oxopropanal
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pentane-2,4-dione + O2
acetate + 2-oxopropanal
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i.e. acetylacetone
i.e. acetate and acetone
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no substrate: 4-hydroxy-4-methyl-2-pentanone, 3-oxobutanoate, quercetin, catechols, 2,4`-dihydroxyacetophenone, ascorbate
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additional information
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the catalytic reaction proceeds via one common rate-limiting step in the clevage of all substrates accepted by the enzyme
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additional information
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residues Arg80 and Tyr70 promote O2 reduction
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additional information
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the enzyme is a mononuclear non-heme iron enzymes, Dke1 active site modelling, overview
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additional information
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acetylacetone dioxygenase catalyzes the dioxygen-dependent degradation of beta-dicarbonyl compounds
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additional information
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Dke1 also performs the atypical cleavage of the alpha-keto acid, 4-hydroxyphenylpyruvate, to form 4-hydroxybenzaldehyde as product instead of the homogentisate product found for 4-hydroxyphenylpyruvate with 4-hydroxyphenylpyruvate dioxygenase, EC 1.13.11.27, analysis of the bonding of the alpha-keto acid, 4-hydroxyphenylpyruvate, to ferrous Dke1 using anaerobic Dke1, added ferrous ammonium sulfate, and 4-hydroxyphenylpyruvate at pH 7.0, overview
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additional information
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Ni(II)-complex-adducts show regioselective oxidative cleavage of the aliphatic C-C bond using dioxygen via the substrate activation mechanism without changing the oxidation state of nickel(II) as similar to the wild type enzyme
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additional information
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iron(II) complexes [Fe(L)(CH3CN)3](SO3CF3)2 of tris(2-pyridyl)-based ligands exhibit very similar chemical surroundings to the active site of the enzyme and mimic its functions
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