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Literature summary for 3.5.1.116 extracted from

  • Shin, I.; Percudani, R.; Rhee, S.
    Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana (2012), J. Biol. Chem., 287, 18796-18805.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.116

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type seleno-L-methionine-substituted, N-terminally His-tagged enzyme and enzyme mutants in Escherichia coli strain BL21(DE3) Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
seleno-L-methionine-substituted wild-type or N-terminally truncated mutant enzymes, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 50 mM Tris, pH 7.4, 1 mM MnCl2, and 5 mM DTT, with crystallization solution containing 0.1 M phosphate citrate, pH 4.2, 10% w/v PEG 3000, 0.2 M NaCl or with 0.1 M HEPES, pH 7.5, 7% w/v PEG 8000, 8% v/v ethylene glycol, 22°C, X-ray diffraction structure determination and analysis at 3.30 A resolution, molecular replacement, molecular modeling Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
E235A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
E235Q site-directed mutagenesis, inactive mutant Arabidopsis thaliana
H237A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
H241A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
K291A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
Q275A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
Y287A site-directed mutagenesis, inactive mutant Arabidopsis thaliana
Y287F site-directed mutagenesis, inactive mutant Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.77
-
 (S)-ureidoglycolate pH 7.4, 30°C, wild-type enzyme Arabidopsis thaliana
2.3
-
 (S)-ureidoglycolate pH 7.4, 30°C, Y252F Arabidopsis thaliana
3.46
-
 (S)-ureidoglycolate pH 7.4, 30°C, K291R Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Arabidopsis thaliana 5783
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ substrate (S)-ureidoglycine is bound to the Mn2+ ion at the active site of homooctameric enzyme. 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] Comment Organism
30200
-
 8 * 30200, SDS-PAGE, an octameric functional unit Arabidopsis thaliana
200000
-
 above, gel filtration Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8VXY9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant seleno-L-methionine-substituted, N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity chromatography, tag cleavage by TEV protease, followed by dialysis and gel filtration Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-ureidoglycolate + H2O substrate (S)-ureidoglycine is bound to the Mn2+ ion at the active site of homooctameric enzyme, conversion of (S)-ureidoglycine into (S)-ureidoglycolate in an enantioselective manner, binding mode, overview Arabidopsis thaliana glyoxylate + 2 NH3 + CO2
-
 ?

Subunits

Subunits Comment Organism
homooctamer 8 * 30200, SDS-PAGE, an octameric functional unit Arabidopsis thaliana
More the monomer structure is in the bicupin fold of the beta-barrel Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
(S)-ureidoglycine aminohydrolase
-
 Arabidopsis thaliana
UGLYAH
-
 Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Arabidopsis thaliana

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
73
-
 (S)-ureidoglycolate pH 7.4, 30°C, Y252F Arabidopsis thaliana
493
-
 (S)-ureidoglycolate pH 7.4, 30°C, K291R Arabidopsis thaliana
761
-
 (S)-ureidoglycolate pH 7.4, 30°C, wild-type enzyme Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism (S)-ureidoglycine aminohydrolase plays a key role in the ureide pathway of purine catabolism of plants and some bacteria Arabidopsis thaliana
additional information the Mn2+ ion acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. Kinetic analysis characterizes the functional roles of the active site residues, including the Mn2+ ion binding site and residues in the vicinity of (S)-ureidoglycine, structure of the enzyme and its possible catalytic mechanism, overview. The crystal structure of monomeric AtUGlyAH, which contains the ordered residues Pro39 to Leu298, is composed of 19 beta-strands and 4 short 310-helices. Residues Tyr287 and Lys291 are essential for enzyme activity, possibly by dictating the orientation of the ureido and carboxyl groups of the substrate, respectively Arabidopsis thaliana

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
32
-
 (S)-ureidoglycolate pH 7.4, 30°C, Y252F Arabidopsis thaliana
143
-
 (S)-ureidoglycolate pH 7.4, 30°C, K291R Arabidopsis thaliana
429
-
 (S)-ureidoglycolate pH 7.4, 30°C, wild-type enzyme Arabidopsis thaliana