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Information on EC 4.3.2.3 - ureidoglycolate lyase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32459

for references in articles please use BRENDA:EC4.3.2.3
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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.3 ureidoglycolate lyase
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.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P32459
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Word Map
  • 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
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
peptidylglycine alpha-amidating monooxygenase, ugl, peptidyl-alpha-hydroxyglycine alpha-amidating lyase, ureidoglycolate lyase, ureidoglycolase, ureidoglycolate urea-lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ureidoglycolate lyase, releasing urea
-
(-)-ureidoglycolate urea-lyase
-
-
-
-
lyase, ureidoglycolate
-
-
-
-
UGL
-
-
-
-
ureidoglycolase
-
-
-
-
ureidoglycolatase
-
-
-
-
ureidoglycolate hydrolase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
-
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
glyoxylate + urea
show the reaction diagram
nickel-dependent urea-release activity
-
-
?
ureidoglycolate
glyoxylate + urea
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
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
nickel-dependent urea-release activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ni2+
nickel-dependent urea-release activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
complete inhibition
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6.0: about 40% of maximal activity, pH 9.0: about 20% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene dal3
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
DAL3 deletion abolishes the activity on ureidoglycolate
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21727
-
x * 21727, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 21727, calculation from nucleotide sequence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene DAL3, the DAL metabolic gene cluster, the so called degradation of allantoin locus, is located on chromosome IX
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Choi, K.S.; Lee, K.W.; Roush, A.H.
The assay of yeast ureidoglycolatase
Anal. Biochem.
17
413-422
1966
Cyberlindnera jadinii, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Yoo, H.; Cooper, T.G.
The ureidoglycollate hydrolase (DAL3) gene in Saccharomyces cerevisiae
Yeast
7
693-698
1991
Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Escherichia coli (P63486), Escherichia coli, Saccharomyces cerevisiae (P32459), Saccharomyces cerevisiae
Manually annotated by BRENDA team