Information on EC 3.5.3.9 - allantoate deiminase

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

EC NUMBER
COMMENTARY hide
3.5.3.9
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RECOMMENDED NAME
GeneOntology No.
allantoate deiminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
allantoate + H2O = (S)-ureidoglycine + NH3 + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of amidines
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
allantoin degradation to ureidoglycolate II (ammonia producing)
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Microbial metabolism in diverse environments
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Purine metabolism
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allantoin degradation
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Arthrobacter allantoicus
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-
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Manually annotated by BRENDA team
ATCC29604
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
Streptococcus allantoicus
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
main enzyme involved in allantoate degradation in common bean
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
(S)-ureidoglycolate + 2 NH3 + CO2
show the reaction diagram
allantoate + 2 H2O
ureidoglycolate + 2 NH3 + CO2
show the reaction diagram
allantoate + 3 H2O
glyoxylate + 4 NH3 + 2 CO2
show the reaction diagram
-
-
-
-
?
allantoate + H2O
(S)-ureidoglycine + NH3 + CO2
show the reaction diagram
allantoate + H2O
ureidoglycine + NH3 + CO2
show the reaction diagram
allantoate + H2O
ureidoglycolate + CO2 + NH3
show the reaction diagram
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-
-
-
?
additional information
?
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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 + 2 H2O
(S)-ureidoglycolate + 2 NH3 + CO2
show the reaction diagram
allantoate + 2 H2O
ureidoglycolate + 2 NH3 + CO2
show the reaction diagram
allantoate + 3 H2O
glyoxylate + 4 NH3 + 2 CO2
show the reaction diagram
-
-
-
-
?
allantoate + H2O
(S)-ureidoglycine + NH3 + CO2
show the reaction diagram
allantoate + H2O
ureidoglycine + NH3 + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
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can replace Mn2+, 85% of activity measured in the presence of Mn2+
Ni2+
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can replace Mn2+, 32% of activity measured in the presence of Mn2+
sulfate
an allosteric effector responsible for stabilizing substrate binding
Zn2+
two co-catalytic zinc ions at the active site governs catalytic specificity for hydrolysis of N-carbamyl versus the peptide bond in exopeptidases, binding structure, the two zinc ions have subtly different coordination geometries, overview
additional information
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Mg2+, Ca2+, Cu2+, Co2+ and Fe2+ can not replace Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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21% inhibition at 1 mM
Acetohydroxamate
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Allantoate
Borate
Cd2+
Streptococcus allantoicus
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at pH 6.5
diethyldicarbonate
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Fe2+
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0.15 mM completely inhibits incubation mixture with Mn2+
fluoride
glycolate
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50% activity loss with 0.06 mM glycolate for 10 min at 30C; strong inhibitor, 50% inhibition at 0.06 mM
glyoxylate
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50% activity loss with 0.02 mM glycolate for 10 min at 30C; strong inhibitor, 50% inhibition at 0.02 mM
guanidine
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10% and 80% activity loss with 2 M and 5 M L-guanidine pre-treatment for 10 min at 30C
hydroxylamine
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67% inhibition at 1 mM
iminourea
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pre-treatment with 2mM or 5mM results in a loss of acitivity of 10% or 80% of activity
L-Asn
L-Asp
N-Acetylimidazole
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5.6% activity loss with 10 mM n-acetylimidazole 10 min at 30C
N-bromosuccinimide
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100% activity loss with 10 mM n-bromosuccinimide for 10 min at 30C; pre-treatment completely inhibits activity
NEM
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15% inhibition at 5 mM
Ni2+
Streptococcus allantoicus
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at pH 6.5
nitrate
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inhibits the nezyme, overview
pyridoxal 5'-phosphate
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pre-treatment with 10 mM completely inhibits activity
pyridoxal-5-phosphate
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100% activity loss with 10 mM pyridoxal-5-phosphate for 10 min at 30C
SDS
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50% activity loss with 50 mM SDS pre-treatment for 10 min at 30C; pre-treatment with 50 mM results in a loss of acitivity of 50% of activity
Urea
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5% and 20% activity loss with 2 M and 5 M urea pre-treatment for 10 min at 30C
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Dinitrophenylhydrazine
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can partially substitute for phenylhydrazine, 67% of the activity with phenylhydrazine
glutathione
L-arginine
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can partially substitute for phenylhydrazine, 19% of the activity with phenylhydrazine
L-lysine
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can partially substitute for phenylhydrazine, 29% of the activity with phenylhydrazine
phenylhydrazine
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completely dependent on phenylhydrazine, which acts as an activator at low concentrations and decreases the affinity of the enzyme for the substrate at higher concentrations, the activation is reduced by pyridoxamine-5'-phosphate and pyridoxal-5'-phosphate
tryptophan
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additional information
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phenylhydrazine crucial for enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.076 - 76
Allantoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18
Allantoate
Phaseolus vulgaris
A6YS26
at pH 8.0 and 40C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032 - 0.0425
fluoride
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004
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ungerminated seeds
0.00138
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crude extract from seedlings; in crude extract after first purification
0.0018
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6-d-old seedlings
0.365
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partially purified enzyme
0.776
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579fold purified enzyme from seedlings
0.8
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after 579-fold purification
1
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vmax of partially purified ADE2 pool
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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activity is maximal in the buffers triethanolamine, TES, HEPES, or phosphate, and 25% lower in MES buffer
7.3
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13500
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gel filtration; gel filtration on Sephacryl S-200 column
50000
x * 50000, mature enzyme, SDS-PAGE
51900
A9GYV1
x * 51900, SDS-PAGE
52400
x * 52400, calculated from amino acid sequence
53100
x * 53100, SDS-PAGE
66000
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2 * 66000, SDS-PAGE
100000
A9GYV1
gel filtration
103000
gel filtration
128000
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nonedenaturating PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ternary complex of allantoate amidohydrolase with substrate allantoate and a sulfate ion, X-ray diffraction structure determination and analysis at 2.25 A resolution, modelling
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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treatment for 15 min reveals a loss of 15% of acitivity
65
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30 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
preparation of allantoate amidohydrolase stabilized by the addition of 0.1 mM EDTA
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reversibly denatured by urea, guanidine and SDS
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, partially purified enzyme, retains the activity for 11 days
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-30C, 2 months, 5% loss of activity
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-30C, Tris-HCl buffer, pH 7.5, 2 months
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4C, 1 week, 10% loss of activity
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4C, partially purified enzyme, retains the activity for 4 days
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4C, Tris-HCl buffer, pH 7.5, 1 week
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55C, 15 min, 15% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
579fold purified ond DEAE-Sephadex column, ADE2 pool; gel filtration with Sephacryl S-200 and Sephadex A50 columns, and dialysis against Tris-HCl pH 7.5 at 4C
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native enzyme 22.4fold by ultracentrifugation and batch separation using an anion exchanger resin
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recombinant StrepII-tagged enzyme from Nicotiana tabacum leaf extracts to homogeneity by streptavidin affinity chromatography
StrepTactin Sepharose column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana benthamiana and Escherichia coli strain BL21(DE3)
expression in Saccharomyces cerevisiae pDR196 and introduced in Saccharomyces cerevisiae mutant dal2 strain
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overexpression in Escherichia coli
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transient expression in Nicotiana tabacum as StrepII-tagged enzyme using the Agrobacterium tumefaciens transfection method
A9GYV1
transient expression in Nicotiana tabacum as StrepII-tagged enzyme using the Agrobacterium tumefaciens transfection method, co-expression of YFP-tagged enzyme in Nicotiana tabacum plants with endoplasmic reticulum and peroxisomal markers
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of AAH transcript is reduced to about 50% in roots after 10 days of drought stress
expression of AAH transcript remains almost at constant levels in shoots and leaves of drought-stressed plants
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
an N-terminally truncated version of AAH-YFP lacking the first 71 amino acids exclusively localized to the cytosol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
Show AA Sequence (168 entries)
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