BRENDA - Enzyme Database
show all sequences of 1.13.11.54

Metal-dependent function of a mammalian acireductone dioxygenase

Deshpande, A.R.; Wagenpfeil, K.; Pochapsky, T.C.; Petsko, G.A.; Ringe, D.; Biochemistry 55, 1398-1407 (2016)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
Ni- and Co-bound proteins. Both Ni and Co present an octahedral coordination geometry in the active site bound to protein ligands H88, H90, H133 and E94. Additionally, two distinct water (or hydroxide) ligands bind to the metal ion center
Mus musculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1185
-
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
Mus musculus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Mus musculus
Fe2+
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Mus musculus
Mn2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Mus musculus
additional information
the identity of bound metal ion does not affect the oligomeric state of ARD
Mus musculus
Ni2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Mus musculus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
23000
26000
gel filtration
Mus musculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mus musculus
Q99JT9
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
i.e. desthio-acireductone
741923
Mus musculus
2-oxovalerate + formic acid
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 21500, calculated
Mus musculus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
43
-
Mn2+ bound enzyme, melting temperature
Mus musculus
58
-
Ni2+ bound enzyme, melting temperature
Mus musculus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
111.7
-
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
Mus musculus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
Ni- and Co-bound proteins. Both Ni and Co present an octahedral coordination geometry in the active site bound to protein ligands H88, H90, H133 and E94. Additionally, two distinct water (or hydroxide) ligands bind to the metal ion center
Mus musculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1185
-
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
Mus musculus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Mus musculus
Fe2+
Ni2+ bound ARD is the most stable followed by Co2+ and Fe2+, and Mn2+-bound ARD being the least stable
Mus musculus
Mn2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Mus musculus
additional information
the identity of bound metal ion does not affect the oligomeric state of ARD
Mus musculus
Ni2+
the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53
Mus musculus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
23000
26000
gel filtration
Mus musculus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(1Z)-1,2-dihydroxyhex-1-en-3-one + O2
i.e. desthio-acireductone
741923
Mus musculus
2-oxovalerate + formic acid
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 21500, calculated
Mus musculus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
43
-
Mn2+ bound enzyme, melting temperature
Mus musculus
58
-
Ni2+ bound enzyme, melting temperature
Mus musculus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
111.7
-
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
Mus musculus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
950
-
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
Mus musculus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
950
-
(1Z)-1,2-dihydroxyhex-1-en-3-one
Fe2+ bound enzyme, pH 7.0, 25°C
Mus musculus
Other publictions for EC 1.13.11.54
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)
743725
Deshpande
Dual chemistry catalyzed by h ...
Homo sapiens
Protein Eng. Des. Sel.
30
197-204
2017
-
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1
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1
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1
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1
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1
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2
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1
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741923
Deshpande
Metal-dependent function of a ...
Mus musculus
Biochemistry
55
1398-1407
2016
-
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1
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1
-
5
1
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1
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1
1
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2
1
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1
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1
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5
1
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1
1
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2
1
-
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-
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1
1
743184
Chang
Interaction between hepatic m ...
Homo sapiens
J. Viral Hepat.
23
256-266
2016
-
1
-
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1
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3
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2
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1
1
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-
-
742270
Valdez
-
Co2+ acireductone dioxygenase ...
Klebsiella oxytoca
Chem. Phys. Lett.
604
77-82
2014
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1
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1
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1
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725214
Allpress
Regioselective aliphatic carbo ...
Klebsiella oxytoca
J. Am. Chem. Soc.
135
659-668
2013
-
-
-
1
-
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1
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1
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1
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1
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1
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1
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1
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1
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2
2
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-
725438
Friedman
Acireductone dioxygenase 1 (AR ...
Arabidopsis thaliana, Arabidopsis thaliana Columbia-0
J. Biol. Chem.
286
30107-30118
2011
1
-
1
-
1
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1
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4
-
6
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1
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4
1
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1
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1
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1
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1
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4
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1
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4
1
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2
2
-
-
-
685212
Chai
Characterization of metal bind ...
Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724
Biochemistry
47
2428-2438
2008
-
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1
-
9
-
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1
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2
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1
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9
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1
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675408
Ju
One protein, two enzymes revis ...
Mus musculus
J. Mol. Biol.
363
823-834
2006
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-
1
-
1
-
-
-
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1
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1
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1
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1
1
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1
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1
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1
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1
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1
1
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-
663098
Sauter
The immediate-early ethylene r ...
Oryza sativa
Plant J.
44
718-729
2005
-
-
1
-
-
-
-
2
-
1
-
1
-
2
-
-
1
-
-
2
-
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2
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-
2
-
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1
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2
-
1
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1
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1
-
2
-
-
2
-
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-
-
2
-
-
-
-
-
-
-
-
-
-
673849
Hirano
Membrane-type 1 matrix metallo ...
Homo sapiens, Saccharomyces cerevisiae, Saccharomyces cerevisiae Y700
Genes Cells
10
565-574
2005
-
-
-
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2
-
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4
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3
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2
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3
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661058
Dai
Mechanistic studies of two dio ...
Klebsiella pneumoniae
Biochemistry
40
6379-6387
2001
-
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-
-
2
-
1
2
1
-
1
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1
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3
1
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2
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2
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1
2
1
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1
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3
1
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2
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662101
Dai
One protein, two enzymes ...
Klebsiella oxytoca
J. Biol. Chem.
274
1193-1195
1999
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1
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2
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1
1
1
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1
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1
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2
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1
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2
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1
1
1
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1
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2
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