Information on EC 3.5.1.116 - ureidoglycolate amidohydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.116
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RECOMMENDED NAME
GeneOntology No.
ureidoglycolate amidohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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hydrolysis of linear amidines
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
allantoin degradation to glyoxylate II
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Metabolic pathways
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Microbial metabolism in diverse environments
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Purine metabolism
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allantoin degradation
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SYSTEMATIC NAME
IUBMB Comments
(S)-ureidoglycolate amidohydrolase (decarboxylating)
This plant enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. Not to be confused with EC 4.3.2.3, ureidoglycolate lyase, which releases urea rather than ammonia.
CAS REGISTRY NUMBER
COMMENTARY hide
115629-07-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-ureidoglycolate + H2O
(S)-ureidoglycolate + 2 NH3
show the reaction diagram
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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
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-
?
(S)-ureidoglycolate + H2O
2 NH3 + CO2 + glyoxylate
show the reaction diagram
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
show the reaction diagram
(S)-ureidoglycolate + H2O
glyoxylate + NH3 + CO2
show the reaction diagram
ureidoglycolate + H2O
glyoxylate + NH3 + CO2
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-ureidoglycolate + H2O
2 NH3 + CO2 + glyoxylate
show the reaction diagram
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
show the reaction diagram
-
-
-
-
?
(S)-ureidoglycolate + H2O
glyoxylate + NH3 + CO2
show the reaction diagram
ureidoglycolate + H2O
glyoxylate + NH3 + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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slight increase of activity
Fe2+
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slight increase of activity
Mg2+
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slight increase of activity
Zn2+
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activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ni2+
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slight
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0113 - 840
(S)-ureidoglycolate
0.085 - 5.4
ureidoglycolate
additional information
additional information
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steady-state kinetic analysis of wild-type and mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 761
(S)-ureidoglycolate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 430
(S)-ureidoglycolate
1342
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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at pH 7.0 and 37C
64
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at pH 7.0 and 37C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
7.5 - 8.5
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8.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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from developing bean
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30200
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8 * 30200, SDS-PAGE, an octameric functional unit
200000
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above, gel filtration
300000
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gel filtration
additional information
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enzyme forms a complex with allantoate amidohydrolase
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
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8 * 30200, SDS-PAGE, an octameric functional unit
additional information
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the monomer structure is in the bicupin fold of the beta-barrel
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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, 22C, X-ray diffraction structure determination and analysis at 3.30 A resolution, molecular replacement, molecular modeling
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wild-type enzyme and mutant E183A complexed with substrate, reaction intermediate, and product, sitting 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 buffer of 0.1 M 4-morpholineethanesulfonic acid, pH 6.5, and 12% w/v PEG 20000, at 22C, crystals of the AtUAH binary complex with substrate or reaction intermediate by co-crystallization of mutant E183A with a (S)-ureidoglycolate, from a crystallization solution containing 0.2 M calcium acetate hydrate, 20% w/v PEG 3350, 1 mM MnCl2, and 5 or 2 mM, respectively, (S)-ureidoglycolate, X-ray diffraction structure determination and analysis at 1.45-2.20 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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15 min, in absence of Mn2+, 60% loss of activity
50
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15 min, in abesence of Mn2+, 88% loss of activity
60
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15 min, in presence of 2 mM Mn2+, stable
70
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15 min, in presence of 2 mM Mn2+, 97% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Mn2+ stabilizes against heat inactivation
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant seleno-L-methionine-substituted, N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by immobilized metal affinity achromatography, tag cleavage by TEV protease, followed by dialysis and gel filtration
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana benthamiana leaf epidermal cells
recombinant expression of seleno-L-methionine-substituted, N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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recombinant expression of wild-type seleno-L-methionine-substituted, N-terminally His-tagged enzyme and enzyme mutants in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D149A
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site-directed mutagenesis, inactive mutant
D149N
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site-directed mutagenesis, inactive mutant
D351A
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site-directed mutagenesis, inactive mutant
E183A
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site-directed mutagenesis, inactive mutant; site-directed mutagenesis, inactive mutant, crystal structure analysis
E183D
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site-directed mutagenesis, inactive mutant
E183Q
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site-directed mutagenesis, inactive mutant
E184A
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site-directed mutagenesis, inactive mutant
E235A
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site-directed mutagenesis, inactive mutant
E235Q
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site-directed mutagenesis, inactive mutant
H138A
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site-directed mutagenesis, inactive mutant
H237A
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site-directed mutagenesis, inactive mutant
H241A
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site-directed mutagenesis, inactive mutant
H254A
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site-directed mutagenesis, inactive mutant
H290A
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site-directed mutagenesis, inactive mutant
H290N
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site-directed mutagenesis, inactive mutant
H290Q
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enyzme
H424N
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enyzme
H448A
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site-directed mutagenesis, inactive mutant
K291A
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site-directed mutagenesis, inactive mutant
N340A
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site-directed mutagenesis, almost inactive mutant
N340D
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site-directed mutagenesis, inactive mutant
Q257A
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site-directed mutagenesis, inactive mutant
Q257E
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site-directed mutagenesis, inactive mutant
Q257N
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enyzme
Q275A
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site-directed mutagenesis, inactive mutant
R353A
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site-directed mutagenesis, inactive mutant
R353K
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site-directed mutagenesis, inactive mutant
Y287A
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site-directed mutagenesis, inactive mutant
Y287F
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site-directed mutagenesis, inactive mutant
Y423A
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site-directed mutagenesis, inactive mutant
Y423F
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enyzme
additional information
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conferring an allantoate amidinohydrolase-like activity on the enzyme by redesigning the size of the (S)-ureidoglycolate amidohydrolase active site and modifying the substrate specifiicty is not successfull by simply relieving the possible steric hindrance of Tyr423 to the incoming pro-S ureido group in allantoate.The AtUAH Y423G mutant is inactive with allantoate. Substrate specificity in the (S)-ureidoglycolate amidohydrolase is a function of interactions more complex than those conferred by a single active-site residue