Information on EC 3.5.2.5 - allantoinase

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

EC NUMBER
COMMENTARY hide
3.5.2.5
-
RECOMMENDED NAME
GeneOntology No.
allantoinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-allantoin + H2O = allantoate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
allantoin degradation
-
-
allantoin degradation to ureidoglycolate I (urea producing)
-
-
allantoin degradation to ureidoglycolate II (ammonia producing)
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Purine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-allantoin amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-20-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NH-Rockefeller strain
UniProt
Manually annotated by BRENDA team
Aedes aegypti NH-Rockefeller
NH-Rockefeller strain
UniProt
Manually annotated by BRENDA team
peanut
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
gene pucH
UniProt
Manually annotated by BRENDA team
pigeonpea
-
-
Manually annotated by BRENDA team
safflower
-
-
Manually annotated by BRENDA team
cat flea
-
-
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
tobacco
-
-
Manually annotated by BRENDA team
castor bean
-
-
Manually annotated by BRENDA team
a nonureide-type legume black locust, gene RpALN
Uniprot
Manually annotated by BRENDA team
male and female brown trout
-
-
Manually annotated by BRENDA team
serovar typhimurium LT2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
corn
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-allantoin + H2O
allantoate
show the reaction diagram
5-ethyl-hydantoin + H2O
?
show the reaction diagram
allantoic acid
(S)-allantoin + H2O
show the reaction diagram
-
-
-
r
allantoin + H2O
allantoate
show the reaction diagram
dihydrouracil + H2O
?
show the reaction diagram
hydantoin + H2O
?
show the reaction diagram
additional information
?
-
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
(S)-allantoin + H2O
allantoate
show the reaction diagram
allantoin + H2O
allantoate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
activates, most effective metal cofactor, inverting the enantioselectivity of AllBali
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
5 mM
4-hydroxymercuribenzoate
-
inactivation, prevented by DTT
5-amino-4-imidazole-carboxamide hydrochloride
-
8-Hydroxyquinoline-5-sulfonic acid
complete inhibition
Acetohydroxamic acid
-
Ca2+
-
62% residual activity at 1 mM for IsoI and 34% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII
Co2+
-
40% residual activity at 1 mM for IsoI and 30% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII
diethyl dicarbonate
-
89% residual activity at 10 mM for IsoI and 90% residual activity at 10 mM for IsoII
dihydroorotate
-
competitive inhibition
dithiothreitol
DTT
complete inhibition
EDTA
-
49% residual activity at 1 mM for IsoI and 40% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII, Fe2+ and Mn2+ restore the enzyme activity partially, while Ca2+ restores it completely
Fe2+
-
75% residual activity at 1 mM for IsoI and 58% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII
H2O2
allosteric effect of H2O2 toward allantoinase
hydantoin
iodoacetic acid
-
16% residual activity at 5 mM for IsoI and 13% residual activity at 5 mM for IsoII
kaempferol
-
-
L-cysteine
complete inhibition
Mg2+
-
44% residual activity at 1 mM for IsoI and 49% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII
Mn2+
-
81% residual activity at 1 mM for IsoI and 51% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII
myricetin
-
-
N-ethylmaleimide
Na+
-
51% residual activity at 1 mM for IsoI and 43% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII
p-chloromercuribenzene sulfonic acid
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
10% residual activity at 0.5 mM for IsoI and 15% residual activity at 0.5 mM for IsoII
quercetin
-
-
Zn2+
-
29% residual activity at 1 mM for IsoI and 38% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-mercaptoethanol
-
14% increase of activity at 0.1 mM for IsoI and 11% increase of activity at 1 mM for IsoII
diethyl dicarbonate
-
63% increase of activity at 0.1 mM for IsoI and 38% increase of activity at 1 mM for IsoII
dithiothreitol
-
20% increase of activity at 1 mM for IsoI and% increase of activity at 0.1 mM for IsoII
phenyl phosphoramidate
-
4% increase of activity at 1 mM for IsoI and 10% increase of activity at 1 mM for IsoII
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26 - 231.6
(S)-allantoin
2.4
Allantoic acid
-
0.059 - 13.8
allantoin
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2 - 24.4
(S)-allantoin
201.7 - 420
allantoin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 1.4
(S)-allantoin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.237 - 0.795
dithiothreitol
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.6
dihydroorotate
Salmonella enterica
-
pH 8.0, 25C, recombinant enzyme
230
hydantoin
Salmonella enterica
-
pH 8.0, 25C, recombinant enzyme
0.035
kaempferol
Salmonella enterica
-
pH 8.0, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
-
-
0.037
-
-
0.08
-
pH 7.5
0.5
-
pH 7.5
1
-
wild-type seedlings grown on Murashige Skoog medium
1.3
Ni2+-activated enzyme, pH 8.0, 25C
2
-
crude extract
2.6
Zn2+-activated enzyme, pH 8.0, 25C
5
seedlings grown on Murashige Skoog medium
8
Co2+-activated enzyme, pH 8.0, 25C
10
-
wild-type seedlings grown on ALN medium
76.1
-
pH 7.4, 37C, Zn2+-amended culture
88.2
Mn2+-activated enzyme, pH 8.0, 25C
295
-
purified isozyme IsoII
400
-
after 200fold purification
410
-
pH 7.4, 37C, Co2+-amended culture
563
-
purified isozyme IsoI
additional information
-
activity of isozymes in different bean tissues and during development, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.7
-
-
7.5 - 7.6
-
-
7.7
-
different methods
7.8 - 8
-
-
7.8
-
different methods; IsoI
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
Mn2+-activited enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
; the amount of IsoII is very low in roots
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
wood, high expression level in bark/cambial region, which is upregulated n spring, but no expression in the sapwood-heartwood transition zone
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Escherichia coli (strain K12)
Pseudomonas fluorescens (strain Pf0-1)
Pseudomonas fluorescens (strain Pf0-1)
Pseudomonas fluorescens (strain Pf0-1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
IsoII, native PAGE with acrylamide gradient; IsoII, SDS-PAGE, after purification two peaks of 45000 and 42000 Da length showing allantoinase activity are obtained
44000
-
gel filtration; SDS-PAGE and gel-filtration
45000
-
IsoI, SDS-PAGE, after purification two peaks of 45000 and 42000 Da length showing allantoinase activity are obtained
50000
-
gel filtration
53300
-
calculated from cDNA
57150
gel filtration
93600
gel filtration
125000
-
gel filtration
140000 - 150000
-
gel filtration
140000
gel filtration, estimated molecular mass
170000 - 215000
gel filtration
189500
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
monomer
tetramer
-
4 * 38000, SDS-PAGE
additional information
gel filtration chromatography reveals a mixture of monomers, dimers, and tetramers
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
different glycosylation stages as well as signal peptide cleavage lead to different subunits sizes of 53 kDa and 56 kDa
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml 14 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 20% w/v PEG 3350, and 0.1 M potassium thiocyanate, pH 6.5, equilibration against 0.5 ml reservoir solution, 20C, X-ray diffraction structure determination and analysis at 3.5 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
no loss in activity over 6 h
60 - 70
-
the activity of both protein variants IsoI and IsoII is very resistant to heat treatment because the enzyme is fully active after treatment for 30 min at 60C and shows more than 50% activity after 30 min at 70C
68
-
7 min, 78% in activity retained
90
-
60 min, 71% of activity at 30C
additional information
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxycholate
-
20% increase of activity in the presence of 0.1% (w/v) deoxycholate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM potassium phosphate buffer, pH 7.5, 15% glycerol, 5 weeks
-
0-5C, 2 weeks, little loss in activity
-
4C, 40 mM phosphate buffer, pH 7, 0.01% sodium azide, 1 mM beta-mercaptoethanol, 4 months
-
8C, 3 weeks, 90% of activity retains
-
frozen state, 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; native enzyme from seeds
-
DEAE-Sephacel column chromatography, MonoQ HR column chromatography, and Sephacryl S-300 gel filtration; native isozymes 1 and 2 from developing fruits 150fold and 286fold, respectively, to homogeneity involving heat treatment at 55C for 20 min, anion exchange chromatography, gel filtration, and another step of anion exchange chromatography
-
recombinant by gel filtration and affinity chromatography to near homogeneity
-
recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, ultrafiltration, and dialysis
recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography, gel fltration, and ultrafiltration
Sephacryl S-200 column gel filtration chromatography at 0-4C
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned from a hindgut and Malpighian tubule library, DNA and amino acid sequence determination and analysis, sequence comparisons
-
expression in Escherichia coli strain BL21
expression in Saccharomyces cerevisiae; expression in Spodoptera frugiperda
-
gene aln, transient expression in Nicotiana tabacum in the endoplasmic reticulum, occasionally also in the Golgi apparatus or the peroxisomes
-
gene AtALN, located on chromosome 4, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional complementation of an enzyme-deficient yeast dal1 mutant
-
gene pucH, DNA and amino acid sequence determination and analysis, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3)
gene RpALN, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression analysis, functional complementation of an enzyme-deficient yeast dal1 mutant
overproduction of enzyme in Escherichia coli
-
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant overexpression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
at the onset of flowering, allantoinase gene expression and enzyme increase in shoots and leaves from plants using symbiotically fixed nitrogen as the sole nitrogen source activity
-
the genes involved in the conversion of allantoin into allantoate and in the deamination of guanine to xanthine are organized in three transcriptional units, hpxSAB, hpxC, and guaD. hpxSAB, which includes hpxB encoding allantoinase, is the most tightly regulated unit. This operon is activated by growth on allantoin as a nitrogen source. Addition of allantoin to nitrogen excess cultures does not result in hpxSAB induction. Full induction of hpxSAB by allantoin requires both HpxS, encoding a regulatory protein of the GntR family, and nitrogen assimilation control protein NAC
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D319A
site-directed mutagenesis, inactive mutant, altered thermal denaturation compared to the wild-type enzyme
D319N
site-directed mutagenesis, inactive mutant, altered thermal denaturation compared to the wild-type enzyme
S292A
site-directed mutagenesis, the mutant shows reduced activity and altered thermal denaturation compared to the wild-type enzyme
T155A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T155Y
site-directed mutagenesis, the mutant shows reduced activity and altered thermal denaturation compared to the wild-type enzyme
D319A
-
site-directed mutagenesis, inactive mutant, altered thermal denaturation compared to the wild-type enzyme
-
D319N
-
site-directed mutagenesis, inactive mutant, altered thermal denaturation compared to the wild-type enzyme
-
S292A
-
site-directed mutagenesis, the mutant shows reduced activity and altered thermal denaturation compared to the wild-type enzyme
-
T155A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
T155Y
-
site-directed mutagenesis, the mutant shows reduced activity and altered thermal denaturation compared to the wild-type enzyme
-
D315A
complete loss of activity
D315N
no activity
H186A
complete loss of activity
H242A
complete loss of activity
H59A
complete loss of activity
H61A
complete loss of activity
K146A
complete loss of activity
N94D
no activity
N94V
no activity
R215K
no significant effect on enzyme activity
S288D
no significant effect on enzyme activity
S288V
no significant effect on enzyme activity
S317D
no activity
S317V
no activity
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant ALLase exhibits no activity but can be activated when preincubating with some metal ions before analyzing its activity. Renaturation follows in decreasing order Mn2+, Co2+, Zn2+, Ni2+, Cd2+, Mg2+
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