Information on EC 4.3.2.3 - ureidoglycolate lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.3.2.3
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RECOMMENDED NAME
GeneOntology No.
ureidoglycolate lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-ureidoglycolate = glyoxylate + urea
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidation
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elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
allantoin degradation to glyoxylate I
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allantoin degradation to glyoxylate III
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Metabolic pathways
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Purine metabolism
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SYSTEMATIC NAME
IUBMB Comments
(S)-ureidoglycolate urea-lyase (glyoxylate-forming)
This microbial enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. Not to be confused with EC 3.5.1.116, ureidoglycolate amidohydrolase, which releases ammonia rather than urea.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-57-7
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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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Manually annotated by BRENDA team
chickpea
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Manually annotated by BRENDA team
Escherichia coli O157:H7 EDL933
O157:H7 EDL933
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-
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
W200
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
mackerel
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
DAL3 deletion abolishes the activity on ureidoglycolate
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)-benzoyl-alpha-hydroxyglycine
glyoxylate + benzamide
show the reaction diagram
-
2% of activity with (S)-ureidoglycolate
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?
(S)-cinnamoyl-alpha-hydroxyglycine
glyoxylate + cinnamamide
show the reaction diagram
-
5.5% of activity with (S)-ureidoglycolate
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?
(S)-ureidoglycolate
glyoxylate + urea
show the reaction diagram
1-naphtylacetyl-alpha-hydroxyglycine
glyoxylate + 1-naphtaleneacetamide
show the reaction diagram
-
2.3% of activity with (S)-ureidoglycolate
-
?
3-phenylpropionyl-alpha-hydroxyglycine
glyoxylate + 3-phenylpropylacetamide
show the reaction diagram
-
1.0% of activity with (S)-ureidoglycolate
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?
4'-methoxyphenylacetyl-alpha-hydroxyglycine
glyoxylate + 4'-methoxyphenylacetamide
show the reaction diagram
-
1.3% of activity with (S)-ureidoglycolate
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?
4'-nitrophenylacetyl-alpha-hydroxyglycine
glyoxylate + 4'-nitrophenylacetamide
show the reaction diagram
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0.5% of activity with (S)-ureidoglycolate
-
?
phenylacetyl-alpha-hydroxyglycine
glyoxylate + phenylacetamide
show the reaction diagram
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0.8% of activity with (S)-ureidoglycolate
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?
ureidoglycolate
?
show the reaction diagram
ureidoglycolate
glyoxylate + urea
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
glyoxylate + urea
show the reaction diagram
ureidoglycolate
?
show the reaction diagram
ureidoglycolate
glyoxylate + urea
show the reaction diagram
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-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Acetopyruvate
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benzoylpyruvate
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Fe2+
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strong inactivation
maleamic acid
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N-acetylphenylpyruvate
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o-phenanthroline
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-asparagine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
(-)-ureidoglycolate
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30C, pH 7.8, in the presence of 0.5 mM Mn2+
0.5
(S)-ureidoglycolate
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30C, pH 7.0
0.03
1-naphtylacetyl-alpha-hydroxyglycine
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30C, pH 7.0
0.04
3-phenylpropionyl-alpha-hydroxyglycine
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30C, pH 7.0
0.09
4'-nitrophenylacetyl-alpha-hydroxyglycine
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30C, pH 7.0
0.028
4-methoxyphenylacetyl-alpha-hydroxyglycine
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30C, pH 7.0
0.09
benzoyl-alpha-hydroxyglycine
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30C, pH 7.0
0.025
cinnamoyl-alpha-hydroxyglycine
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30C, pH 7.0
0.024
phenylacetyl-alpha-hydroxyglycine
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30C, pH 7.0
0.33 - 17
ureidoglycolate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
ureidoglycolate
Phaseolus vulgaris
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50 mM Tes, pH 7.8, 0.5 mM MnSO4, 3 mM phenylhydrazine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00056
Acetopyruvate
-
30C, pH 7.0
0.0000022
benzoylpyruvate
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30C, pH 7.0
11.6
maleamic acid
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30C, pH 7.0
0.0012
N-acetylphenylpyruvate
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30C, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.439
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50 mM Tes, pH 7.8, 0.5 mM MnSO4, 3 mM phenylhydrazine
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.6
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pH 6.5: about 50% of maximal activity, pH 8.6: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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activity assay
70
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and above, chemical instability of ureidoglycolate at higher temperatures
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
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approx. 30% of maximal activity at 40C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
121000
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sucrose density gradient centrifugation
180000
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gel filtration
240000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 21727, calculation from nucleotide sequence
hexamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; 1.7 A resolution, sitting drops method
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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15 min, in presence of Mn2+, complete inactivation
80
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no loss of activity after 60 min in the presence of Mn2+
90
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complete loss of activity after 40 min in the presence of Mn2+
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10 mM Tris-HCl, pH 8.0, 0.1 M NaCl, 10% glycerol, stable for at least 3 months
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-20C, stable for 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; Ni-NTA affinity chromatography
ammonium sulfate precipitation, gel filtration, heat treatment, hydrophobic interaction chromatography, immunoaffinity chromatography
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ammonium sulfate, gel filtration, heat treatment, ion exchange, electrophoresis
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DEAE-Sephacel, oxamate affinity, Superose
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liver enzyme
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partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression as a C-terminal His6-tag fusion protein
gene allA, encoded in the ALL locus
gene DAL3, the DAL metabolic gene cluster, the so called degradation of allantoin locus, is located on chromosome IX
into the pCIS vector for transfection of CHO cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the locus encoding the enzyme is expressed under anaerobiosis and nitrogen starvation
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S767A
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mutant is engineered to lack the N-glycosylation site at Asn765
Y582F
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mutant is engineered for analysing the role of the thyrosine residues for the activity of the enzyme
Y595F
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mutant is engineered for analysing the role of the thyrosine residues for the activity of the enzyme
Y654F
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mutant is engineered for analysing the role of the thyrosine residues for the activity of the enzyme
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