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show all sequences of 1.13.11.50

Spectroscopic and computational studies of alpha-keto acid binding to Dke1: understanding the role of the facial triad and the reactivity of beta-diketones

Diebold, A.R.; Straganz, G.D.; Solomon, E.I.; J. Am. Chem. Soc. 133, 15979-15991 (2011)

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
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
Acinetobacter johnsonii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Acinetobacter johnsonii
acetylacetone dioxygenase catalyzes the dioxygen-dependent degradation of beta-dicarbonyl compounds
?
-
-
-
pentane-2,4-dione + O2
Acinetobacter johnsonii
-
acetate + methylglyoxal
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acinetobacter johnsonii
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
acetylacetone dioxygenase catalyzes the dioxygen-dependent degradation of beta-dicarbonyl compounds
725198
Acinetobacter johnsonii
?
-
-
-
-
additional information
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
725198
Acinetobacter johnsonii
?
-
-
-
-
pentane-2,4-dione + O2
-
725198
Acinetobacter johnsonii
acetate + methylglyoxal
-
-
-
?
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
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
Acinetobacter johnsonii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Acinetobacter johnsonii
acetylacetone dioxygenase catalyzes the dioxygen-dependent degradation of beta-dicarbonyl compounds
?
-
-
-
pentane-2,4-dione + O2
Acinetobacter johnsonii
-
acetate + methylglyoxal
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
acetylacetone dioxygenase catalyzes the dioxygen-dependent degradation of beta-dicarbonyl compounds
725198
Acinetobacter johnsonii
?
-
-
-
-
additional information
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
725198
Acinetobacter johnsonii
?
-
-
-
-
pentane-2,4-dione + O2
-
725198
Acinetobacter johnsonii
acetate + methylglyoxal
-
-
-
?
General Information
General Information
Commentary
Organism
additional information
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. active site was modeling, histidine residues are truncated to methyl imidazole for the model, and constraints imposed by the protein backbone are simulated by fixing the relative positions of the beta-carbons of the backbone. The coordination of the active site is completed with either alpha keto (monoanion) or enolate (dianion) bidentate coordinated 4-hydroxyphenylpyruvate ligand or a monoanionic acetylacetone ligand
Acinetobacter johnsonii
General Information (protein specific)
General Information
Commentary
Organism
additional information
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. active site was modeling, histidine residues are truncated to methyl imidazole for the model, and constraints imposed by the protein backbone are simulated by fixing the relative positions of the beta-carbons of the backbone. The coordination of the active site is completed with either alpha keto (monoanion) or enolate (dianion) bidentate coordinated 4-hydroxyphenylpyruvate ligand or a monoanionic acetylacetone ligand
Acinetobacter johnsonii
Other publictions for EC 1.13.11.50
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Insight of the iron binding a ...
Acinetobacter johnsonii
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88
297-306
2015
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1
3
-
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725553
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Dke1--structure, dynamics, and ...
Acinetobacter johnsonii
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17
801-815
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4
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10
1
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2
2
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725198
Diebold
Spectroscopic and computationa ...
Acinetobacter johnsonii
J. Am. Chem. Soc.
133
15979-15991
2011
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711258
Diebold
The three-his triad in Dke1: c ...
Acinetobacter johnsonii
Biochemistry
49
6945-6952
2010
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711267
Straganz
Kinetic and CD/MCD spectroscop ...
Acinetobacter johnsonii
Biochemistry
49
996-1004
2010
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9
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1
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1
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1
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1
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3
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1
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10
1
1
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9
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1
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1
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10
1
1
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696107
Leitgeb
Biochemical characterization a ...
Acinetobacter johnsonii
Biochem. J.
418
403-411
2009
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1
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8
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6
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6
1
1
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2
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1
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1
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4
1
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1
1
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8
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6
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6
1
1
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4
1
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675466
Straganz
-
Exploring the cupin-type metal ...
Acinetobacter johnsonii
J. Mol. Catal. B
39
171-178
2006
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1
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1
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2
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1
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1
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657614
Hofer
Fast determination of operatio ...
Acinetobacter johnsonii
Appl. Microbiol. Biotechnol.
1
1-12
2005
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1
1
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1
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2
1
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657866
Grogan
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Acinetobacter johnsonii
Biochem. J.
388
721-730
2005
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1
1
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1
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6
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671683
Straganz
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Integrated approach for produc ...
Acinetobacter johnsonii
Biocatal. Biotransform.
23
261-269
2005
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1
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3
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4
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674150
Straganz
Reaction coordinate analysis f ...
Acinetobacter johnsonii
J. Am. Chem. Soc.
127
12306-12314
2005
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4
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1
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1
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4
1
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4
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636327
Straganz
Acetylacetone-cleaving enzyme ...
Acinetobacter johnsonii
Biochem. J.
369
573-581
2003
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1
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5
1
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1
1
1
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3
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1
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11
1
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11
1
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1
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636328
Straganz
A novel beta-diketone-cleaving ...
Acinetobacter johnsonii
Biochem. Biophys. Res. Commun.
297
232-236
2002
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