BRENDA - Enzyme Database
show all sequences of 1.13.11.54

The immediate-early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine

Sauter, M.; Lorbiecke, R.; Ouyang, B.; Pochapsky, T.C.; Rzewuski, G.; Plant J. 44, 718-729 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Oryza sativa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1
-
O2
-
Oryza sativa
25.9
-
1,2-dihydroxy-3-oxopent-1-ene
-
Oryza sativa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
bacterially expressed AsARD1 preferentially binds Fe2+ rather than Ni2+
Oryza sativa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Oryza sativa
OsARD1 is a primary ethylene response gene. Enzyme catalyzes the penultimate step in the methionine cycle.
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oryza sativa
-
indica cultivar Pin Gaew 56
-
Purification (Commentary)
Commentary
Organism
recombinant
Oryza sativa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
internode
strongly induced in adventitious roots and in the youngest internode of partially submerged plants
Oryza sativa
-
root
strongly induced in adventitious roots and in the youngest internode of partially submerged plants
Oryza sativa
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihydroxy-3-oxopent-1-ene + O2
-
663098
Oryza sativa
2-oxo-butanoate + formate
-
-
-
?
additional information
OsARD1 is a primary ethylene response gene. Enzyme catalyzes the penultimate step in the methionine cycle.
663098
Oryza sativa
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11.7
-
1,2-dihydroxy-3-oxopent-1-ene
-
Oryza sativa
11.8
-
O2
-
Oryza sativa
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Oryza sativa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1
-
O2
-
Oryza sativa
25.9
-
1,2-dihydroxy-3-oxopent-1-ene
-
Oryza sativa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
bacterially expressed AsARD1 preferentially binds Fe2+ rather than Ni2+
Oryza sativa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Oryza sativa
OsARD1 is a primary ethylene response gene. Enzyme catalyzes the penultimate step in the methionine cycle.
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant
Oryza sativa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
internode
strongly induced in adventitious roots and in the youngest internode of partially submerged plants
Oryza sativa
-
root
strongly induced in adventitious roots and in the youngest internode of partially submerged plants
Oryza sativa
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,2-dihydroxy-3-oxopent-1-ene + O2
-
663098
Oryza sativa
2-oxo-butanoate + formate
-
-
-
?
additional information
OsARD1 is a primary ethylene response gene. Enzyme catalyzes the penultimate step in the methionine cycle.
663098
Oryza sativa
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11.7
-
1,2-dihydroxy-3-oxopent-1-ene
-
Oryza sativa
11.8
-
O2
-
Oryza sativa
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
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30
197-204
2017
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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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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
1
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2
1
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1
1
743184
Chang
Interaction between hepatic m ...
Homo sapiens
J. Viral Hepat.
23
256-266
2016
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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
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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
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1
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1
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1
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4
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6
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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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-
685212
Chai
Characterization of metal bind ...
Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724
Biochemistry
47
2428-2438
2008
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1
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9
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1
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2
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9
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675408
Ju
One protein, two enzymes revis ...
Mus musculus
J. Mol. Biol.
363
823-834
2006
-
-
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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663098
Sauter
The immediate-early ethylene r ...
Oryza sativa
Plant J.
44
718-729
2005
-
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1
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2
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1
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1
-
2
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2
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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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661058
Dai
Mechanistic studies of two dio ...
Klebsiella pneumoniae
Biochemistry
40
6379-6387
2001
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2
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1
2
1
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1
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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
-
-
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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