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Information on EC 4.3.2.3 - ureidoglycolate lyase
for references in articles please use BRENDA:EC4.3.2.3
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IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
- 4.3.2.3
- pituitary
-
neuropeptide
-
cooh-terminal
-
glycine-extended
-
endoproteolytic
-
alpha-hydroxylating
-
1.14.17.3
-
prohormone
-
neurointermediate
-
corticotrope
-
ascorbate-dependent
-
glucuronyl
-
granule-associated
-
cuproenzymes
-
beta-monooxygenase
- allantoicase
-
uteroglobin
showSynonyms
peptidylglycine alpha-amidating monooxygenase, ugl, peptidyl-alpha-hydroxyglycine alpha-amidating lyase, ureidoglycolate lyase, ureidoglycolase, ureidoglycolate urea-lyase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(-)-ureidoglycolate urea-lyase
allA
lyase, ureidoglycolate
-
-
-
-
UGL
ureidoglycolase
-
-
-
-
ureidoglycolatase
-
-
-
-
ureidoglycolate hydrolase
ureidoglycolate lyase, releasing urea
YbbT
(-)-ureidoglycolate urea-lyase
-
-
-
-
UGL
-
-
-
-
ureidoglycolate hydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-ureidoglycolate = glyoxylate + urea
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
C-N-bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
allantoin degradation to glyoxylate I, allantoin degradation to glyoxylate III
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9014-57-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-benzoyl-alpha-hydroxyglycine
glyoxylate + benzamide
-
Substrates: 2% of activity with (S)-ureidoglycolate
Products: -
Products: -
?
(S)-cinnamoyl-alpha-hydroxyglycine
glyoxylate + cinnamamide
-
Substrates: 5.5% of activity with (S)-ureidoglycolate
Products: -
Products: -
?
1-naphtylacetyl-alpha-hydroxyglycine
glyoxylate + 1-naphtaleneacetamide
-
Substrates: 2.3% of activity with (S)-ureidoglycolate
Products: -
Products: -
?
3-phenylpropionyl-alpha-hydroxyglycine
glyoxylate + 3-phenylpropylacetamide
-
Substrates: 1.0% of activity with (S)-ureidoglycolate
Products: -
Products: -
?
4'-methoxyphenylacetyl-alpha-hydroxyglycine
glyoxylate + 4'-methoxyphenylacetamide
-
Substrates: 1.3% of activity with (S)-ureidoglycolate
Products: -
Products: -
?
4'-nitrophenylacetyl-alpha-hydroxyglycine
glyoxylate + 4'-nitrophenylacetamide
-
Substrates: 0.5% of activity with (S)-ureidoglycolate
Products: -
Products: -
?
benzoyl-alpha-hydroxyglycine
glyoxylate + benzamide
-
Substrates: -
Products: -
Products: -
?
cinnamoyl-alpha-hydroxyglycine
glyoxylate + cinnamamide
-
Substrates: -
Products: -
Products: -
?
phenylacetyl-alpha-hydroxyglycine
glyoxylate + phenylacetamide
-
Substrates: 0.8% of activity with (S)-ureidoglycolate
Products: -
Products: -
?
(S)-ureidoglycolate
glyoxylate + urea
Substrates: nickel-dependent urea-release activity
Products: -
Products: -
?
(S)-ureidoglycolate
glyoxylate + urea
-
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate
glyoxylate + urea
Substrates: nickel-dependent urea-release activity
Products: -
Products: -
?
ureidoglycolate
?
-
Substrates: enzyme is involved in purine degradation
Products: -
Products: -
?
ureidoglycolate
?
-
Substrates: enzyme is involved in allantoin degradation
Products: -
Products: -
?
ureidoglycolate
?
-
Substrates: enzyme is involved in purine degradation
Products: -
Products: -
?
ureidoglycolate
?
-
Substrates: enzyme is involved in degradation of xanthine
Products: -
Products: -
?
ureidoglycolate
glyoxylate + urea
-
Substrates: ?
Products: -
Products: -
?
ureidoglycolate
glyoxylate + urea
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: recombinant enzyme from Escherichia coli is unable to release ammonia directly from ureidoglycolate
Products: -
Products: -
?
additional information
?
-
-
Substrates: recombinant enzyme from Escherichia coli is unable to release ammonia directly from ureidoglycolate
Products: -
Products: -
?
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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
glyoxylate + urea
Substrates: nickel-dependent urea-release activity
Products: -
Products: -
?
(S)-ureidoglycolate
glyoxylate + urea
-
Substrates: -
Products: -
Products: -
?
(S)-ureidoglycolate
glyoxylate + urea
Substrates: nickel-dependent urea-release activity
Products: -
Products: -
?
ureidoglycolate
?
-
Substrates: enzyme is involved in purine degradation
Products: -
Products: -
?
ureidoglycolate
?
-
Substrates: enzyme is involved in allantoin degradation
Products: -
Products: -
?
ureidoglycolate
?
-
Substrates: enzyme is involved in purine degradation
Products: -
Products: -
?
ureidoglycolate
?
-
Substrates: enzyme is involved in degradation of xanthine
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Ni2+
Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
complete inhibition, 50% of activity is restored after removal of EDTA, addition of Mn2+, Zn2+ or Mg2+ recover the activity to the initial levels
EDTA
complete inhibition, the activity can only be rescued by an excess of Ni2+ ions, not by other metal ions, i.e. Ca2+, Co2+, Cu2+, Mg2+, Mn2+, Zn2+, and Fe2+
EDTA
-
10 mM, complete inhibition, activity can be restored by Mn2+ and Co2+, slightly by Zn2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
Amidation inhibitors 4-phenyl-3-butenoic acid and 5-(acetylamino)-4-oxo-6-phenyl-2-hexenoic acid methyl ester are novel HDAC inhibitors with anti-tumorigenic properties.
Carcinoma
Androgen-independent expression of adrenomedullin and peptidylglycine alpha-amidating monooxygenase in human prostatic carcinoma.
Carcinoma
Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase.
Coma
Hyaluronic acid derived from other streptococci supports Streptococcus pneumoniae in vitro biofilm formation.
Glioblastoma
Neutralization of adrenomedullin inhibits the growth of human glioblastoma cell lines in vitro and suppresses tumor xenograft growth in vivo.
Glioma
Neutralization of adrenomedullin inhibits the growth of human glioblastoma cell lines in vitro and suppresses tumor xenograft growth in vivo.
Menkes Kinky Hair Syndrome
In vitro copper stimulation of plasma peptidylglycine alpha-amidating monooxygenase in Menkes disease variant with occipital horns.
Multiple Sclerosis
Increased peptidylglycine alpha-amidating monooxygenase activity in cerebrospinal fluid of patients with multiple sclerosis.
Neoplasms
Molecular analysis integrating different pathways associated with androgen-independent progression in LuCaP 23.1 xenograft.
Pheochromocytoma
Identification of potential gene markers and insights into the pathophysiology of pheochromocytoma malignancy.
Pheochromocytoma
Regulation of carboxypeptidase E by membrane depolarization in PC12 pheochromocytoma cells: comparison with mRNAs encoding other peptide- and catecholamine-biosynthetic enzymes.
Pituitary Neoplasms
Peptidylglycine alpha-amidating monooxygenase (PAM) immunoreactivity and messenger RNA in human pituitary and increased expression in pituitary tumours.
Prostatic Neoplasms
Catalytically active peptidylglycine alpha-amidating monooxygenase in the media of androgen-independent prostate cancer cell lines.
Seizures
Interactions of peptide amidation and copper: Novel biomarkers and mechanisms of neural dysfunction.
Thyroid Neoplasms
Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.9
ureidoglycolate
-
50 mM Tes, pH 7.8, 0.5 mM MnSO4, 3 mM phenylhydrazine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
ureidoglycolate
-
50 mM Tes, pH 7.8, 0.5 mM MnSO4, 3 mM phenylhydrazine
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
6.5 - 8.6
-
pH 6.5: about 50% of maximal activity, pH 8.6: about 40% of maximal activity
6 - 9
-
pH 6.0: about 40% of maximal activity, pH 9.0: about 20% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
and above, chemical instability of ureidoglycolate at higher temperatures
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
detoxification of the reaction product glyoxylate in the peroxisomes by the malate synthase reaction
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
malfunction
DAL3 deletion abolishes the activity on ureidoglycolate
additional information
additional information
the AllA structure reveals two gracious small barrel (cupin) folds
additional information
-
the AllA structure reveals two gracious small barrel (cupin) folds
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
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