Information on EC 3.5.3.4 - allantoicase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.5.3.4
-
RECOMMENDED NAME
GeneOntology No.
allantoicase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
allantoate + H2O = (S)-ureidoglycolate + urea
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amidines
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
allantoin degradation to ureidoglycolate I (urea producing)
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
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Purine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
allantoate amidinohydrolase
Also hydrolyses (R)-ureidoglycolate to glyoxylate and urea.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-21-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
female mosquitoes; NH-Rockefeller strain
SwissProt
Manually annotated by BRENDA team
Aedes aegypti NH-Rockefeller
NH-Rockefeller strain
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Mantis sp.
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Penicillium citreo-viride
-
-
-
Manually annotated by BRENDA team
prawn
-
-
-
Manually annotated by BRENDA team
enzyme also has allantoinase activity, EC 3.5.2.5
-
-
Manually annotated by BRENDA team
mackerel
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-ureidoglycolate
glyoxylate + urea
show the reaction diagram
(-)-ureidoglycolate + urea
allantoate + H2O
show the reaction diagram
-
-
-
r
allantoate + H2O
(-)-ureidoglycolate + urea
show the reaction diagram
allantoate + H2O
(S)-ureidoglycolate + urea
show the reaction diagram
allantoate + H2O
?
show the reaction diagram
-
-
-
-
-
allantoate + H2O
ureidoglycolate + urea
show the reaction diagram
allantoic acid + H2O
ureidoglycolate + urea
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
allantoate + H2O
?
show the reaction diagram
-
-
-
-
-
allantoic acid + H2O
ureidoglycolate + urea
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Bivalent cations
-
-
Co2+
required for maximum activity
Ni2+
required for maximum activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(-)-ureidoglycolate
-
-
Allantoate
-
with (-)-ureidoglycolate as substrate
Ca2+
1 mM, about 50% of inhibition, reversed by EDTA
diethyldicarbonate
-
-
glycolic acid
Hydantoic acid
-
-
iodoacetate
-
slight
Mg2+
1 mM, about 50% of inhibition, reversed by EGTA
N-Acetylimidazole
-
-
N-Carbamoyl-(R)-asparagine
-
-
p-hydroxymercuribenzoate
-
-
additional information
not inhibitory: Ca2+, Mg2+, EDTA, EGTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
1 mM, more than 200% of initial activity
EGTA
1 mM, about 200% of initial activity
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
(-)-ureidoglycolate
-
-
2 - 250
Allantoate
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
750
Allantoate
Chlamydomonas reinhardtii
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
30C, pH 7.9
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Mantis sp.
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000
-
sedimentation diffusion equilibrium, 0.9-S-allantoicase
20000
-
SDS-PAGE
43200
-
calculated from sequence of cDNA
154000
-
sedimentation, 10.8-S-allantoicase
200000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
analytical gel filtration
hexamer
monomer
-
X-ray crystallography using the multi-wavelength anomalous dispersion method
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme contains glucosamine
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with allantoate, sitting drop vapor diffusion method, using 0.1 M sodium citrate (pH 5.6), 20% (w/v) polyethylene glycol 4000, 20%(v/v) isopropanol, 1 mMMnCl2, and 5 mM allantoate
; Se-Met-labeled protein crystals grown from a mixture in a 1:1.5 ratio of 8 mg/ml protein solution and a reservoir solution of 7% PEG8000, 12% PEG400, and 100 mM HEPES, pH 7.5
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nanodroplet vapor diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
-
-
172151
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
15 min, loss of about 50% of activity
50
-
34% loss of activity after 30 min, 79% loss of activity after 90 min
75
-
in presence of Mn2+ stable up to 75C, in absence of Mn2+ completely inactivated within 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing, stable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 0.02 M Tris-HCl buffer, pH 7.5, 6 months,
-
-20C, 50 mM phosphate buffer, pH 7.0, stable
4C, above, rapid loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; in the presence of Mn2+ ions and chromatography on Ecteola cellulose at 72C
-
; recombinant enzyme
gravity flow metal chelate column chromatography
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nickel-nitrilotriacetic acid column chromatography and gel filtration on a Superdex 75 column equilibrated in Tris-HCl, pH 7.5, 200 mM NaCl, 10 mM 2-mercaptoethanol
-
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli strain DL41
-
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E126A
inactive
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inhibition by divalent cations is reversed by excess of chaletors of these cations
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
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