Any feedback?
No. of entries
Information on EC 3.5.1.116 - ureidoglycolate amidohydrolase
for references in articles please use BRENDA:EC3.5.1.116
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.1 In linear amides
3.5.1.116 ureidoglycolate amidohydrolase
IUBMB Comments
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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 3.5.1.116
- allantoin
- allantoate
- purine
-
ureide
- ammonia
- glyoxylate
- allantoicase
-
legumes
-
aminohydrolase
- allophanate
showSynonyms
ureidoglycolate amidohydrolase, ureidoglycolate hydrolase, osuah, uglyah, (s)-ureidoglycolate amidohydrolase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amidase, ureidoglycolate
-
-
-
-
EC 3.5.3.19
-
-
formerly
-
UAH
UGDA
-
-
-
-
ureidoglycolate hydrolase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
hydrolysis of linear amidines
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
allantoin degradation to glyoxylate II
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
115629-07-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-ureidoglycolate + H2O
2 NH3 + CO2 + glyoxylate
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
2 NH3 + CO2 + glyoxylate
Substrates: a hydrolytic reaction caused by the attack of water to the amidic bond of ureidoglycolate, with formation of carbamate and hydroxyglycine as primary products
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
2 NH3 + CO2 + glyoxylate
-
Substrates: a hydrolytic reaction caused by the attack of water to the amidic bond of ureidoglycolate, with formation of carbamate and hydroxyglycine as primary products
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
-
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
Substrates: 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
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
Substrates: via the reaction intermediate (S)-hydroxyglycine, enzyme binding structure of substrate, intermediate, and product, overview
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
-
Substrates: -
Products: -
Products: -
?
ureidoglycolate + H2O
glyoxylate + NH3 + CO2
-
Substrates: enzyme plays a role in allantoate catabolism
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: in Arabidopsis, S-ureidoglycolate is hydrolyzed to glyoxylate, carbon dioxide and two molecules of ammonia by UAUAH
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-ureidoglycolate + H2O
2 NH3 + CO2 + glyoxylate
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
-
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate + H2O
glyoxylate + 2 NH3 + CO2
-
Substrates: -
Products: -
Products: -
?
ureidoglycolate + H2O
glyoxylate + NH3 + CO2
-
Substrates: enzyme plays a role in allantoate catabolism
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
Mn2+ is required for maximum catalytic activity. The bimetal reaction center of the enzyme is located at the pocket enclosed by the catalytic domain, dimerization domain, and other structural elements from a different subunit, structure, overview
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetic analysis of wild-type and mutant enzymes
-
additional information
additional information
-
steady-state kinetic analysis of wild-type and mutant enzymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
sequences of endoplasmic reticulum-targeting signals comprise residues 1-25
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
additional information
metabolism
(S)-ureidoglycine aminohydrolase plays a key role in the ureide pathway of purine catabolism of plants and some bacteria
metabolism
the enzyme is involved in the plant ureide pathway, overview
additional information
amino acid and structure comparisons, e.g. to allantoate amidinohydrolase, enzyme monomer structure modeling, overview. Monomeric AtUAH (Asn54 to Asp476) is composed of 13 alpha-helices, 12 beta-strands, and 2 short 310-helices. It folds largely into two structural domains: a catalytic domain (residues 54-275 and 392-476) and a dimerization domain (residues 276-391) that is inserted between beta6 and alpha11 of the catalytic domain. The two structural domains are connected by a so-called hinge region (residues 273-275 and 392-394), structure-function analysis, overview. The catalytic domain exhibits an alpha/beta/alpha-folded architecture. Substrate specificity in the (S)-ureidoglycolate amidohydrolase is a function of interactions more complex than those conferred by a single active-site residue
additional information
-
amino acid and structure comparisons, e.g. to allantoate amidinohydrolase, enzyme monomer structure modeling, overview. Monomeric AtUAH (Asn54 to Asp476) is composed of 13 alpha-helices, 12 beta-strands, and 2 short 310-helices. It folds largely into two structural domains: a catalytic domain (residues 54-275 and 392-476) and a dimerization domain (residues 276-391) that is inserted between beta6 and alpha11 of the catalytic domain. The two structural domains are connected by a so-called hinge region (residues 273-275 and 392-394), structure-function analysis, overview. The catalytic domain exhibits an alpha/beta/alpha-folded architecture. Substrate specificity in the (S)-ureidoglycolate amidohydrolase is a function of interactions more complex than those conferred by a single active-site residue
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
Show AA Sequence and Transmembrane Helices (676 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the monomer structure is in the bicupin fold of the beta-barrel
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, 22Ā°C, X-ray diffraction structure determination and analysis at 3.30 A resolution, molecular replacement, molecular modeling
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 22Ā°C, 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E183A
H290Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H424N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q257N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y423F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
E183A
site-directed mutagenesis, inactive mutant, crystal structure analysis
additional information
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
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
recombinant expression of wild-type seleno-L-methionine-substituted, N-terminally His-tagged enzyme and enzyme mutants in Escherichia coli strain BL21(DE3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
low-temperature-induced expression of rice ureidoglycolate amidohydrolase is mediated by a C-repeat/dehydration-responsive element that specifically interacts with rice C-repeat-binding factor 3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wells, X.E.; Lees, E.M.
Ureidoglycolate amidohydrolase from developing French bean fruits (Phaseolus vulgaris [L.].)
Arch. Biochem. Biophys.
287
151-159
1991
Phaseolus vulgaris
brenda
Winkler, R.G.; Blevins, D.G.; Randall, D.D.
Ureide catabolism in soybean. III. Ureidoglycolate amidohydrolase and allantoate amidohydrolase are activities of an allantoate degrading enzyme complex
Plant Physiol.
86
1084-1088
1988
Glycine max
brenda
Werner, A.; Romeis, T.; Witte, C.
Ureide catabolism in Arabidopsis thaliana and Escherichia coli
Nat. Chem. Biol.
6
19-21
2010
Arabidopsis thaliana
brenda
Werner, A.K.; Medina-Escobar, N.; Zulawski, M.; Sparkes, I.A.; Cao, F.Q.; Witte, C.P.
The ureide-degrading reactions of purine ring catabolism employ three amidohydrolases and one aminohydrolase in Arabidopsis, soybean, and rice
Plant Physiol.
163
672-681
2013
Arabidopsis thaliana, Glycine max, Oryza sativa
brenda
Percudani, R.; Carnevali, D.; Puggioni, V.
Ureidoglycolate hydrolase, amidohydrolase, lyase: how errors in biological databases are incorporated in scientific papers and vice versa
Database (Oxford)
2013
bat071
2013
Glycine max, Arabidopsis thaliana (Q8VXY9), Arabidopsis thaliana
brenda
Shin, I.; Percudani, R.; Rhee, S.
Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana
J. Biol. Chem.
287
18796-18805
2012
Arabidopsis thaliana (Q8VXY9)
brenda
Shin, I.; Han, K.; Rhee, S.
Structural insights into the substrate specificity of (S)-ureidoglycolate amidohydrolase and its comparison with allantoate amidohydrolase
J. Mol. Biol.
426
3028-3040
2014
Arabidopsis thaliana (Q8VXY9), Arabidopsis thaliana
brenda
Li, J.; Qin, R.Y.; Li, H.; Xu, R.F.; Yang, Y.C.; Ni, D.H.; Ma, H.; Li, L.; Wei, P.C.; Yang, J.B.
Low-temperature-induced expression of rice ureidoglycolate amidohydrolase is mediated by a C-repeat/dehydration-responsive element that specifically interacts with rice C-repeat-binding factor 3
Front. Plant Sci.
6
1011
2015
Oryza sativa Japonica Group (Q2QMN7)
brenda
EXTERNAL LINKS (specific for EC-Number 3.5.1.116)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
