BRENDA - Enzyme Database show
show all sequences of 3.5.3.26

Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana

Shin, I.; Percudani, R.; Rhee, S.; J. Biol. Chem. 287, 18796-18805 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli B834 and BL21 (DE3) cells
Arabidopsis thaliana
Crystallization (Commentary)
Crystallization
Organism
seleno-L-methionine-labelled enzyme, hanging drop vapor diffusion method, using either 0.1 M phosphate citrate, pH 4.2, 10% (w/v) PEG 3000, 0.2 M NaCl or 0.1 M HEPES, pH 7.5, 7% (w/v) PEG 8000, 8% (v/v) ethylene glycol
Arabidopsis thaliana
Engineering
Amino acid exchange
Commentary
Organism
E235A
inactive
Arabidopsis thaliana
E235Q
inactive
Arabidopsis thaliana
H237A
inactive
Arabidopsis thaliana
H241A
inactive
Arabidopsis thaliana
K291A
inactive
Arabidopsis thaliana
K291R
the mutant shows reduced activity compared to the wild type
Arabidopsis thaliana
Q275A
inactive
Arabidopsis thaliana
Y252F
the mutant shows reduced activity compared to the wild type
Arabidopsis thaliana
Y287A
inactive
Arabidopsis thaliana
Y287F
inactive
Arabidopsis thaliana
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.77
-
(S)-2-ureidoglycine
wild type enzyme, at pH 8.5 and 30°C
Arabidopsis thaliana
2.3
-
(S)-2-ureidoglycine
mutant enzyme Y252F, at pH 8.5 and 30°C
Arabidopsis thaliana
3.46
-
(S)-2-ureidoglycine
mutant enzyme K291R, at pH 8.5 and 30°C
Arabidopsis thaliana
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
contains Mn2+, the Mn2+ ion acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction
Arabidopsis thaliana
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30200
-
8 * 30200, SDS-PAGE
Arabidopsis thaliana
200000
-
gel filtration
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-2-ureidoglycine + H2O
Arabidopsis thaliana
-
(S)-ureidoglycolate + NH3
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
Q8GXV5
-
-
Purification (Commentary)
Commentary
Organism
immobilized metal affinity column chromatography and Superdex 200 gel filtration
Arabidopsis thaliana
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-2-ureidoglycine + H2O
-
734179
Arabidopsis thaliana
(S)-ureidoglycolate + NH3
-
-
-
?
Subunits
Subunits
Commentary
Organism
homooctamer
8 * 30200, SDS-PAGE
Arabidopsis thaliana
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
73
-
(S)-2-ureidoglycine
mutant enzyme Y252F, at pH 8.5 and 30°C
Arabidopsis thaliana
493
-
(S)-2-ureidoglycine
mutant enzyme K291R, at pH 8.5 and 30°C
Arabidopsis thaliana
761
-
(S)-2-ureidoglycine
wild type enzyme, at pH 8.5 and 30°C
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli B834 and BL21 (DE3) cells
Arabidopsis thaliana
Crystallization (Commentary) (protein specific)
Crystallization
Organism
seleno-L-methionine-labelled enzyme, hanging drop vapor diffusion method, using either 0.1 M phosphate citrate, pH 4.2, 10% (w/v) PEG 3000, 0.2 M NaCl or 0.1 M HEPES, pH 7.5, 7% (w/v) PEG 8000, 8% (v/v) ethylene glycol
Arabidopsis thaliana
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E235A
inactive
Arabidopsis thaliana
E235Q
inactive
Arabidopsis thaliana
H237A
inactive
Arabidopsis thaliana
H241A
inactive
Arabidopsis thaliana
K291A
inactive
Arabidopsis thaliana
K291R
the mutant shows reduced activity compared to the wild type
Arabidopsis thaliana
Q275A
inactive
Arabidopsis thaliana
Y252F
the mutant shows reduced activity compared to the wild type
Arabidopsis thaliana
Y287A
inactive
Arabidopsis thaliana
Y287F
inactive
Arabidopsis thaliana
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.77
-
(S)-2-ureidoglycine
wild type enzyme, at pH 8.5 and 30°C
Arabidopsis thaliana
2.3
-
(S)-2-ureidoglycine
mutant enzyme Y252F, at pH 8.5 and 30°C
Arabidopsis thaliana
3.46
-
(S)-2-ureidoglycine
mutant enzyme K291R, at pH 8.5 and 30°C
Arabidopsis thaliana
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
contains Mn2+, the Mn2+ ion acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction
Arabidopsis thaliana
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30200
-
8 * 30200, SDS-PAGE
Arabidopsis thaliana
200000
-
gel filtration
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-2-ureidoglycine + H2O
Arabidopsis thaliana
-
(S)-ureidoglycolate + NH3
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
immobilized metal affinity column chromatography and Superdex 200 gel filtration
Arabidopsis thaliana
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-2-ureidoglycine + H2O
-
734179
Arabidopsis thaliana
(S)-ureidoglycolate + NH3
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homooctamer
8 * 30200, SDS-PAGE
Arabidopsis thaliana
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
73
-
(S)-2-ureidoglycine
mutant enzyme Y252F, at pH 8.5 and 30°C
Arabidopsis thaliana
493
-
(S)-2-ureidoglycine
mutant enzyme K291R, at pH 8.5 and 30°C
Arabidopsis thaliana
761
-
(S)-2-ureidoglycine
wild type enzyme, at pH 8.5 and 30°C
Arabidopsis thaliana
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
32
-
(S)-2-ureidoglycine
mutant enzyme Y252F, at pH 8.5 and 30°C
Arabidopsis thaliana
143
-
(S)-2-ureidoglycine
mutant enzyme K291R, at pH 8.5 and 30°C
Arabidopsis thaliana
429
-
(S)-2-ureidoglycine
wild type enzyme, at pH 8.5 and 30°C
Arabidopsis thaliana
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
32
-
(S)-2-ureidoglycine
mutant enzyme Y252F, at pH 8.5 and 30°C
Arabidopsis thaliana
143
-
(S)-2-ureidoglycine
mutant enzyme K291R, at pH 8.5 and 30°C
Arabidopsis thaliana
429
-
(S)-2-ureidoglycine
wild type enzyme, at pH 8.5 and 30°C
Arabidopsis thaliana
Other publictions for EC 3.5.3.26
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)
734179
Shin
Structural and functional insi ...
Arabidopsis thaliana
J. Biol. Chem.
287
18796-18805
2012
-
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1
1
10
-
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3
-
1
2
1
-
3
-
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1
-
-
-
-
-
1
1
-
-
-
3
-
-
-
-
-
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1
-
1
10
-
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-
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3
-
1
2
1
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-
1
-
-
-
-
1
1
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3
-
-
-
-
-
-
-
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3
3
718460
Serventi
Chemical basis of nitrogen rec ...
Arabidopsis thaliana, Escherichia coli
ACS Chem. Biol.
5
203-214
2010
-
-
1
-
-
-
-
-
2
2
-
1
-
7
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-
1
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-
-
-
-
3
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2
-
-
-
2
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1
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2
2
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1
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-
1
-
-
-
-
3
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
720512
Werner
Ureide catabolism in Arabidops ...
Arabidopsis thaliana
Nat. Chem. Biol.
6
19-21
2010
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-
-
-
-
-
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1
-
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4
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1
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-
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-
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1
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1
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