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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Metals Ions
Metals Ions on EC 1.13.11.50 - acetylacetone-cleaving enzyme
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Fe2+
Iron
Ni2+
Zn2+
additional information
Fe2+
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0.9-1.0 iron atoms per subunit, bound to active enzyme, essential for catalytic activity
Fe2+
sulfate, necessary for enzyme activity. About 0.9 mol Fe2+/mol wild-type enzyme, less than 5% Fe2+ in mutants except 0.27 mol/mol H104E-enzyme and 0.45 mol/mol H104N-enzyme
Fe2+
Dke1 contains an atypical, three-histidine-ligated, mononuclear non-heme Fe2+ center, spectroscopic analysis, overview. Stabilizing effect of Glu98 on the 6C geometry of the metal center, priming it for substrate ligation. Also Thr107 stabilizes the Fe(II) cofactor
Fe2+
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the Fe(II) coordinating triad is composed of three His residues, geometric and electronic structure of the Fe(II) center, structure and function comparison with other dioxygenases containing a two histidines and a carboxylate coordinating the iron center in a facial triad, overview
Fe2+
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active site nonheme monoiron(II) center, facially ligated by three histidine residues, overview. Spectral analysis of Dke1 FeII-alpha-keto acid complexes with 4-hydroxyphneylpyruvate, overview
Fe2+
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nonheme Fe(II) cofactor, distinct organization of the hydrophilic triad in the free and substrate-ligated wild-type enzyme. In the free species, the Fe(II) center is coordinated to three histidines and one glutamate, whereas the substrate-ligated, catalytically competent enzyme-substrate complex has an Fe(II) center with three-histidine coordination, with a small fraction of three-histidine, one-glutamate coordination
Fe2+
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its active site consists of a redox-active iron(II) center
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dependent on, metalloenzyme, 1 iron bound per subunit, required for positioning of the substrate and for rendering of the appropriate electronic environment
Iron
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. The Fe2+ ion when expelled from the binding site can be trapped at different locations within the enzyme. The neighborhood of residue Glu11 (form the neighbor subunit) is the second most favorable binding site for the Fe2+ ion after the active site
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the enzyme is a mononuclear non-heme iron enzyme, overview
additional information
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spectrophotometrical monitoring, Fe2+ and Fe3+ coordination, formation of iron(II) enzyme-substrate complexes, and detachment kinetics, overview