Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.4.6 - urea carboxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32528

for references in articles please use BRENDA:EC6.3.4.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.6 urea carboxylase
IUBMB Comments
A biotinyl-protein. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase, thus bringing about the hydrolysis of urea to CO2 and NH3. Previously also listed as EC 3.5.1.45. The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P32528
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
urea amidolyase, dur1,2, urea carboxylase, urea amido-lyase, atp-urea amidolyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP-urea amidolyase
-
DUR1,2
a 1800 amino acid protein with a 600 amino acid amidase domain fused at the N-terminus
ATP:urea amidolyase
-
-
-
-
UALase
-
-
-
-
Urea amido-lyase
-
-
-
-
Urea carboxylase (hydrolysing)
-
-
-
-
Urease (ATP-hydrolysing)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate
show the reaction diagram
a biotinyl-protein, the yeast enzyme (but not that from green algae) also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase, thus bringing about the hydrolysis of urea to CO2 and NH3, previously also listed as EC 3.5.1.45
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
yeast enzyme
decarboxylation
-
-
-
-
Deamination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
urea:carbon-dioxide ligase (ADP-forming)
A biotinyl-protein. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase, thus bringing about the hydrolysis of urea to CO2 and NH3. Previously also listed as EC 3.5.1.45. The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9058-98-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
multifunctional enzyme, catalyzes carboxylation of urea with urea carboxylase, EC 6.3.4.6, and hydrolysis of allophanate with allophanate hydrolase, EC 3.5.1.54
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
show the reaction diagram
-
-
-
ir
urea + H2O + ATP
CO2 + NH3 + ADP + phosphate
show the reaction diagram
in the presence of enzyme, ATP, bicarbonate, magnesium, and potassium ions, ammonium ion is produced from human serum urea
-
-
?
ATP + 2-chloroacetamide + HCO3-
?
show the reaction diagram
-
-
-
-
?
ATP + acetamide + HCO3-
?
show the reaction diagram
-
-
-
-
?
ATP + formamide + HCO3-
?
show the reaction diagram
-
-
-
-
?
ATP + formylurea + HCO3-
?
show the reaction diagram
-
-
-
-
?
ATP + hydantoic acid + HCO3-
?
show the reaction diagram
-
-
-
-
?
ATP + hydroxyurea + HCO3-
?
show the reaction diagram
-
-
-
-
?
ATP + N-methylurea + HCO3-
?
show the reaction diagram
-
-
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
show the reaction diagram
ATP + urethane + HCO3-
?
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
ATP + urea + HCO3-
ADP + phosphate + allophanate
show the reaction diagram
-
-
-
ir
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HCO3-
requirement, hydrolysis of urea
K+
requirement, hydrolysis of urea
Mg2+
requirement, hydrolysis of urea
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
strong, Ca2+ affects the enzyme-ATP-Mg complex by the time of urea carboxylation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
ATP-dependent cleavage of urea
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.39
Urea
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
hydrolysis of urea
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
201665
-
x * 201665, calculation from nucleotide sequence
204000
-
x * 204000, SDS-PAGE, amino acid composition
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
enzymatic assay for measurement of serum urea nitrogen using urea amidolyase
analysis
-
enzymatic assay with urea amidolyase for determination of potassium in serum
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Whitney, P.A.; Cooper, T.G.
Urea carboxylase and allophanate hydrolase. Two components of adenosine triphosphate:urea amido-lyase in Saccharomyces cerevisiae
J. Biol. Chem.
247
1349-1353
1972
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Roon, R.J.; Levenberg, B.
Urea amidolyase. I. Properties of the enzyme from Candida utilis
J. Biol. Chem.
247
4107-4113
1972
Saccharomyces cerevisiae, Debaryomyces subglobosus, Cyberlindnera jadinii, Chlamydomonas reinhardtii, Pseudochlorella pringsheimii, Auxenochlorella pyrenoidosa
Manually annotated by BRENDA team
Whitney, P.A.; Cooper, T.G.
Urea carboxylase and allophanate hydrolase: two components of a multienzyme complex in Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
49
45-51
1972
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Roon, R.J.; Hampshire, J.; Levenberg, B.
Urea amidolyase. The involvement of biotin in urea cleavage
J. Biol. Chem.
247
7539-7545
1972
Saccharomyces cerevisiae, Cyberlindnera jadinii
Manually annotated by BRENDA team
Whitney, P.A.; Cooper, T.
Urea carboxylase from Saccharomyces cerevisiae. Evidence for a minimal two-step reaction sequence
J. Biol. Chem.
248
325-330
1973
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Sumrada, R.A.; Cooper, T.G.
Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast
J. Biol. Chem.
257
9119-9127
1982
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kimura, S.; Iyama, S.; Yamaguchi, Y.; Hayashi, S.; Fushimi, R.; Amino, N.
New enzymatic assay with urea amidolyase for determining potassium in serum
Ann. Clin. Biochem.
34
384-388
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Genbauffe, F.S.; Cooper, T.G.
The urea amidolyase (DUR1,2) gene of Saccharomyces cerevisiae
DNA Seq.
2
19-32
1991
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kimura, S.; Iyama, S.; Yamaguchi, Y.; Kanakura, Y.
New enzymatic assay for serum urea nitrogen using urea amidolyase
J. Clin. Lab. Anal.
17
52-56
2003
Saccharomyces cerevisiae (P32528), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Navarathna, D.H.; Harris, S.D.; Roberts, D.D.; Nickerson, K.W.
Evolutionary aspects of urea utilization by fungi
FEMS Yeast Res.
10
209-213
2010
Eremothecium gossypii, Aspergillus fumigatus, Aspergillus nidulans, Candida albicans, [Candida] glabrata, Fusarium graminearum, Kluyveromyces lactis, Pyricularia grisea, Clavispora lusitaniae, Parastagonospora nodorum, Saccharomyces cerevisiae (P32528)
Manually annotated by BRENDA team