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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.3.4 - allantoicase

for references in articles please use BRENDA:EC3.5.3.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.3 In linear amidines
                3.5.3.4 allantoicase
IUBMB Comments
Also hydrolyses (R)-ureidoglycolate to glyoxylate and urea.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q9JHX6
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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
allantoicase, allantoate amidohydrolase, allantoate amidinohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Allantoate amidinohydrolase
-
-
-
-
Allantoine amidinohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amidines
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
allantoate amidinohydrolase
Also hydrolyses (R)-ureidoglycolate to glyoxylate and urea.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-21-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
allantoate + H2O
(S)-ureidoglycolate + urea
show the reaction diagram
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
not inhibitory: Ca2+, Mg2+, EDTA, EGTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
no activation by EDTA or EGTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
250
Allantoate
pH 7.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALLC_MOUSE
414
0
46294
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46500
x * 47200, deduced from gene sequence, x * 46500, SDS-PAGE
47200
x * 47200, deduced from gene sequence, x * 46500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 47200, deduced from gene sequence, x * 46500, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM phosphate buffer, pH 7.0, stable
4°C, above, rapid loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vigetti, D.; Monetti, C.; Pollegioni, L.; Taramelli, R.; Bernardini, G.
Xenopus allantoicase: Molecular cloning, enzymatic activity and developmental expression
Arch. Biochem. Biophys.
379
90-96
2000
Xenopus laevis, Xenopus laevis (Q9W6S5), Mus musculus (Q9JHX6)
Manually annotated by BRENDA team