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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.1.54 - allophanate hydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32528

for references in articles please use BRENDA:EC3.5.1.54
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate .
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
Reaction Schemes
hide
urea-1-carboxylate
+
H2O
=
2
CO2
+
2
NH3
+
=
2
+
2
Synonyms
allophanate hydrolase, allophanate lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
allophanate lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amides
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
urea-1-carboxylate amidohydrolase
Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9076-72-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
show the reaction diagram
-
-
-
r
allophanate + H2O
CO2 + NH3
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
urea-1-carboxylate + H2O
2 CO2 + 2 NH3
show the reaction diagram
-
-
-
r
allophanate + H2O
CO2 + NH3
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
urea-1-carboxylate
pH 7.3, temperature not specified in the publication, urea amidolyase
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
32
urea-1-carboxylate
pH 7.3, temperature not specified in the publication, urea amidolyase
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
139.13
urea-1-carboxylate
pH 7.3, temperature not specified in the publication, urea amidolyase
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
urea carboxylase (UC) and allophanate hydrolase (A) display a close evolutionary and functional association. The inter-domain coupling efficiency is low in both bacterial and yeast UAL
physiological function
urea amidolyase (UAL) is a multifunctional biotin-dependent enzyme that contributes to both bacterial and fungal pathogenicity by catalyzing the ATP-dependent cleavage of urea into ammonia and CO2. Urea amidolyase is comprised of two enzymatic components: urea carboxylase (UC) and allophanate hydrolase (A)
additional information
urea amidolyase (UAL) comprises two enzymatic components: urea carboxylase (UC) and allophanate hydrolase. The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent. Allophanate is not directly channeled from PsUC to PsAH
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
204000
-
sedimentation analysis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
component of a multienzyme complex, identical, multifunctional subunits
-
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 a multienzyme complex in Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
49
45-51
1972
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
Lin, Y.; Boese, C.; St. Maurice, M.
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Candida albicans (A0A1D8PDC6), Candida albicans ATCC MYA-2876 (A0A1D8PDC6), Granulibacter bethesdensis (Q0BRB0), Granulibacter bethesdensis ATCC BAA-1260 (Q0BRB0), Granulibacter bethesdensis CGDN1H1 (Q0BRB0), Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato ATCC BAA-871D-5, Pseudomonas syringae pv. tomato DC3000, Saccharomyces cerevisiae (P32528), Saccharomyces cerevisiae ATCC 204508 (P32528)
Manually annotated by BRENDA team