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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.3.9 - allantoate deiminase and Organism(s) Escherichia coli and UniProt Accession P77425

for references in articles please use BRENDA:EC3.5.3.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. In plants it is localized in the endoplasmic reticulum. Requires manganese.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P77425
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ataah, allantoate-degrading enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
allantoate amidohydrolase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amidines
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
allantoate amidinohydrolase (decarboxylating)
This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. In plants it is localized in the endoplasmic reticulum. Requires manganese.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-13-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
allantoate + 2 H2O
ureidoglycolate + 2 NH3 + CO2
show the reaction diagram
-
-
-
-
?
allantoate + H2O
(S)-ureidoglycine + NH3 + CO2
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
allantoate + 2 H2O
ureidoglycolate + 2 NH3 + CO2
show the reaction diagram
-
-
-
-
?
allantoate + H2O
(S)-ureidoglycine + NH3 + CO2
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cusa, E.; Obradors, N.; Baldom, L.; Badia, J.; Aguilar, J.
Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli
J. Bacteriol.
181
7497-7484
1999
Escherichia coli
-
Manually annotated by BRENDA team
Serventi, F.; Ramazzina, I.; Lamberto, I.; Puggioni, V.; Gatti, R.; Percudani, R.
Chemical basis of nitrogen recovery through the ureide pathway: Formation and hydrolysis of S-ureidoglycine in plants and bacteria
ACS Chem. Biol.
5
203-214
2010
Escherichia coli (P77425)
Manually annotated by BRENDA team