Information on EC 3.1.3.31 - nucleotidase

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

EC NUMBER
COMMENTARY hide
3.1.3.31
-
RECOMMENDED NAME
GeneOntology No.
nucleotidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a nucleotide + H2O = a nucleoside + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleotide phosphohydrolase
A wide specificity for 2', 3'- and 5'- nucleotides; also hydrolyses glycerol phosphate and 4-nitrophenyl phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-33-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Col-0 wild-type, alx8 mutant, fry1-1 mutant, T-DNA insertional knockout mutant, normal growth conditions and drought stress
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bothrops pradoi
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
formerly Bothrops castelnaudi
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ssp. cascavella; ssp. collilineatus; ssp terrificus
-
-
Manually annotated by BRENDA team
genes surE, yfbR, and yjjG
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ssp. muta
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
wild-type and gPAPP deficient mutants
-
-
Manually annotated by BRENDA team
no activity in Loxosceles gaucho
-
-
-
Manually annotated by BRENDA team
no activity in Philodryas olfersii
-
-
-
Manually annotated by BRENDA team
rainbow trout
-
-
Manually annotated by BRENDA team
Wistar
-
-
Manually annotated by BRENDA team
MB 22, gram-negative, motile
-
-
Manually annotated by BRENDA team
gene xapy
SwissProt
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
2',3'-cyclic-AMP + H2O
adenosine + phosphate
show the reaction diagram
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
2'-GMP + H2O
?
show the reaction diagram
-
-
-
-
?
2'-UMP + H2O
deoxyuridine + phosphate
show the reaction diagram
2-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
2-naphthol phosphate + H2O
2-naphthol + phosphate
show the reaction diagram
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
3'-CMP + H2O
cytidine + phosphate
show the reaction diagram
3'-CMP + H2O
cytosine + phosphate
show the reaction diagram
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
show the reaction diagram
3'-dCMP + H2O
deoxycytidine + phosphate
show the reaction diagram
3'-dTMP + H2O
deoxythymidine + phosphate
show the reaction diagram
3'-dUMP + H2O
deoxyuridine + phosphate
show the reaction diagram
3'-GMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
show the reaction diagram
3'-UMP + H2O
uridine + phosphate
show the reaction diagram
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
5'-AMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
?
5'-ATP + H2O
5'-ADP + phosphate
show the reaction diagram
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
5'-dAMP + H2O
deoxyadenosine + phosphate
show the reaction diagram
5'-dATP + H2O
?
show the reaction diagram
-
i.e. 2'-deoxyadenosine 5'-triphosphate
-
-
?
5'-dCMP + H2O
2'-deoxycytidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
show the reaction diagram
5'-dCTP + H2O
?
show the reaction diagram
-
i.e. 2'-deoxycytidine 5'-triphosphate
-
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
5'-dGTP + H2O
?
show the reaction diagram
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
show the reaction diagram
5'-dIMP + H2O
hypoxanthine + phosphate
show the reaction diagram
-
YfbR
-
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
show the reaction diagram
5'-dUMP + H2O
deoxyuridine + phosphate
show the reaction diagram
5'-GMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
5'-TMP + H2O
thymidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
show the reaction diagram
-
Golgi-resident gPAPP protein has 3'-phosphoadenosine 5'-phosphate-phosphatase activity, functional role of gPAPP protein in the formation of skeletal elements through endochondral ossification in mice
-
-
?
ADP + H2O
?
show the reaction diagram
ADP + H2O
adenosine + diphosphate
show the reaction diagram
low activity
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
AMP + H2O
adenosine + phosphate
show the reaction diagram
ATP + H2O
?
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O
AMP + diphosphate
show the reaction diagram
low activity
-
-
?
CDP + H2O
?
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CMP + H2O
cytosine + phosphate
show the reaction diagram
-
61.7% activity compared to AMP
-
-
?
CTP + H2O
?
show the reaction diagram
-
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
-
-
-
?
cyclic 3',5'-dTMP
?
show the reaction diagram
-
lysosomal enzyme
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
?
dAMP + H2O
deoxyadenosine + phosphate
show the reaction diagram
-
66% activity compared to AMP
-
-
?
dCMP + H2O
deoxycytosine + phosphate
show the reaction diagram
-
12.1% activity compared to AMP
-
-
?
dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
-
49.9% activity compared to AMP
-
-
?
dIMP + H2O
deoxyinosine + phosphate
show the reaction diagram
-
60.9% activity compared to AMP
-
-
?
dsDNA 3' phosphate + H2O
dsDNA + phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
GMP + H2O
guanosine + phosphate
show the reaction diagram
-
33.5% activity compared to AMP
-
-
?
GTP + H2O
?
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
IDP + H2O
?
show the reaction diagram
-
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
IMP + H2O
inosine + phosphate
show the reaction diagram
-
33.1% activity compared to AMP
-
-
?
ITP + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
polyphosphate + H2O
phosphate
show the reaction diagram
-
SurE
-
-
?
TDP + H2O
?
show the reaction diagram
-
-
-
-
?
TMP + H2O
thymidine + phosphate
show the reaction diagram
-
15.2% activity compared to AMP
-
-
?
TTP + H2O
?
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
UDP + H2O
uridine + diphosphate
show the reaction diagram
best substrate, the enzyme shows some specificity for uridine nucleotides
-
-
?
UMP + H2O
uridine + phosphate
show the reaction diagram
-
49.5% activity compared to AMP
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
UTP + H2O
UMP + diphosphate
show the reaction diagram
the enzyme shows some specificity for uridine nucleotides
-
-
?
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
ADP + H2O
adenosine + diphosphate
show the reaction diagram
Q8AVX8
low activity
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
100% activity, 15fold preference for AMP over IMP
-
-
?
ATP + H2O
AMP + diphosphate
show the reaction diagram
Q8AVX8
low activity
-
-
?
dsDNA 3' phosphate + H2O
dsDNA + phosphate
show the reaction diagram
-
repair of DNA-damage
-
-
?
UDP + H2O
uridine + diphosphate
show the reaction diagram
Q8AVX8
best substrate, the enzyme shows some specificity for uridine nucleotides
-
-
?
UTP + H2O
UMP + diphosphate
show the reaction diagram
Q8AVX8
the enzyme shows some specificity for uridine nucleotides
-
-
?
additional information
?
-
-
physiological significance for spleen cytoplasm in the reutilization of nucleotides, especially for thymidine and uridine nucleotides
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
0-50 mM activate
lithium ion
-
in vitro inhibition
Ni2+
-
activates SurE
Sr2+
-
can replace Ca2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-nitrophenyl phosphate
-
49.9% inhibition at 10 mM
5'-deoxy-5'-isobutylthioadenosine
-
21.1% inhibition at 3 mM
5'-deoxy-5'-isobutylthioinosine
-
54.8% inhibition at 7 mM
6-N,N-diethyl-beta-gamma-dibromomethylene-D-adenosine-5-triphosphate
-
i.e. ARL67156, concentrations of 100-300 microM
adenosine
IC50: 0.16 mM
ADP
-
inhibits SurE slightly, YfbR, not YjjG, competitive
beta,gamma-imidoATP
-
the inhibitory respond is blocked by 8-phenyltheophylline and superfusion with adenosine deaminase
citrate
-
lysosomal enzyme
CMP
-
55.4% inhibition at 10 mM
CTP
-
inhibits SurE, YfbR, not YjjG, competitive
D-ribose 5-phosphate
-
14.2% inhibition at 10 mM
dAMP
-
66.1% inhibition at 10 mM
dATP
-
inhibits SurE, YfbR, not YjjG, competitive
dCTP
-
inhibits SurE, YfbR, not YjjG, competitive
deoxyuridine
-
hydrolysis of 5'-dUMP
dGTP
-
inhibits SurE, YfbR, not YjjG, competitive
dTTP
-
inhibits SurE, YfbR, not YjjG, competitive
fluoxetine
-
tricyclic antidepressant, acute and chronic treatment, concentrations of 100, 250, and 500 microM, decreases ATP (17.8%) hydrolysis in hippocampus, decreases ATP (25.5%) hydrolysis in the cerebral cortex, no inhibitory effects on AMP hydrolysis in cerebral cortex and hippocampus
GMP
-
42.7% inhibition at 10 mM
GTP
-
inhibits SurE, YfbR, not YjjG, competitive
IMP
-
36% inhibition at 10 mM
ITP
-
inhibits SurE, YfbR, not YjjG, competitive
LiCl
-
uncompetitive mode of inhibition
malate
-
lysosomal enzyme
Mg2+
-
inhibitory at 10 mM and above
molybdate
IC50: 0.25 mM
NaF
-
strong inhibitor
NaN3
-
inhibits the enzyme from digestive gland by 36% at 0.01 mM, no inhibition of the enzyme from nervous ganglia
NEM
-
inhibits the enzyme from digestive gland by 45%, no inhibition of the enzyme from nervous ganglia
nortriptyline
-
tricyclic antidepressant, acute and chronic treatment, concentrations of 100, 250, and 500 microM, decreases ATP (16.3%) hydrolysis in the hippocampus, increases ATP (32.3%) hydrolysis in the cerebral cortex, no inhibitory effects on AMP hydrolysis in cerebral cortex and hippocampus
oxalate
-
lysosomal enzyme
p-hydroxymercuribenzoate
-
lysosomal enzyme
p-Hydroxymercuriphenylsulfonate
-
lysosomal enzyme
phosphate
PO43-
-
hydrolysis of 5'-dUMP
Tartrate
TTP
-
inhibits SurE, YfbR, not YjjG, competitive
UMP
-
74.5% inhibition at 10 mM
UTP
-
inhibits SurE, YfbR, and slightly YjjG, competitive
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-dGMP
-
activation of hydrolysis of 3'-dTMP
5'-dIMP
-
activation of hydrolysis of 3'-dTMP
5'-dTDP
-
activation of hydrolysis of 3'-dTMP
-
5'-dTMP
-
activation of hydrolysis of 3'-dTMP
5'-dTTP
-
activation of hydrolysis of 3'-dTMP
-
5'-dUMP
-
activation of hydrolysis of 3'-dTMP
cyclic 3',5'-dTMP
-
activation of hydrolysis of 3'-UMP
-
deoxyguanosine
deoxyinosine
deoxythymidine
deoxythymidine 5'-phosphate p-nitrophenyl ester
-
activation of hydrolysis of 3'-dTMP
deoxyuridine
fluoxetine
-
tricyclic antidepressant, concentrations of 100, 250, and 500 microM, chronic treatment increases ADP (80.1%) and AMP (33.3%) hydrolysis, no alteration of enzyme activities by acute treatment
glutamate
-
increases nucleotide hydrolysis at low concentrations (10 and 100 microM), effect counteracted by 2-phenyl-1,2-benzisoselenazol-3(2H)-one (i.e. ebselen), that acts as glutathione peroxidase mimic, or by diphenyl diselenide
Inosine
-
activation
NaCl
-
the PAN-A/1 protein requires high salt for optimal ATPase activity and complex stability. At 1.4 M NaCl, the ATPase activity of PAN-A/1 is reduced to only 43% of activity in the presence of 2 M NaCl. Further reduction of NaCl concentrations to levels of 0.751 M NaCl result in PAN-A/1 protein with only 5-8% of the ATPase activity detected at 2 M NaCl
nortriptyline
-
tricyclic antidepressant, concentrations of 100, 250, and 500 microM, chronic treatment increases ATP (32.3%), ADP (51.8%), and AMP (59.5%) hydrolysis in the cerebral cortex, activation of ADP hydrolysis (49.8%) in acute treatment in cerebral cortex
oligomycin
-
activates the nervous ganglia enzyme
Ouabain
-
activates the nervous ganglia enzyme
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58
2'-AMP
-
lysosomal enzyme
0.22
2'-UMP
-
-
0.016 - 42
3'-AMP
0.05 - 0.53
3'-CMP
1.7
3'-dAMP
-
cytosolic enzyme
1.7
3'-dGMP
-
cytosolic enzyme
0.16 - 2.6
3'-dTMP
0.28 - 8
3'-dUMP
0.044 - 1.7
3'-GMP
0.021 - 0.023
3'-phosphoadenosine 5'-phosphate
0.17 - 0.335
3'-UMP
2.09 - 17.8
4-nitrophenyl phosphate
0.016 - 13
5'-AMP
0.013 - 3.7
5'-CMP
0.012 - 3
5'-dAMP
0.036 - 6.2
5'-dCMP
0.047 - 12
5'-dGMP
0.017 - 4.4
5'-dIMP
0.008 - 3.2
5'-dTMP
0.02 - 14
5'-dUMP
0.011 - 17
5'-GMP
0.089 - 8.6
5'-IMP
0.044 - 7
5'-TMP
0.013 - 95
5'-UMP
0.057 - 0.726
ADP
0.053 - 0.589
ATP
0.36
cyclic 3',5'-dTMP
-
lysosomal enzyme
-
0.534
D-ribose-5-phosphate
37C, pH6
25
Glycerol 2-phosphate
-
cytosolic enzyme
0.18 - 4
p-nitrophenyl phosphate
0.02
Polyphosphate
-
pH 7.0, 37C, SurE, with Mg2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.84 - 160
3'-AMP
5.93 - 188
3'-CMP
0.56 - 4.1
4-nitrophenyl phosphate
4.9 - 173
5'-AMP
0.3
5'-dAMP
-
pH 8.0, 37C, YfbR, with Co2+
0.23
5'-dCMP
-
pH 8.0, 37C, YfbR, with Co2+
0.2 - 8.04
5'-dGMP
0.24
5'-dIMP
-
pH 8.0, 37C, YfbR, with Co2+
0.16 - 30.4
5'-dTMP
0.23 - 21.4
5'-dUMP
11 - 205
5'-GMP
34.2 - 267
5'-UMP
65
D-ribose-5-phosphate
37C, pH6
129
p-nitrophenyl phosphate
37C, pH6
0.05
Polyphosphate
-
pH 7.0, 37C, SurE, with Mg2+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
ADP
-
pH 8.0, 37C, YfbR, versus 5'-dAMP, with Co2+
0.0017 - 0.024
ATP
0.0014
dATP
-
pH 8.0, 37C, YfbR, versus 5'-dAMP, with Co2+
0.174 - 0.211
LiCl
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
adenosine
Elizabethkingia meningoseptica
O08351
IC50: 0.16 mM
0.5
EDTA
Elizabethkingia meningoseptica
O08351
IC50: 0.5 mM
1.5
fluoride
Elizabethkingia meningoseptica
O08351
IC50: 1.5 mM
0.25
molybdate
Elizabethkingia meningoseptica
O08351
IC50: 0.25 mM
0.3
NAD+
Elizabethkingia meningoseptica
O08351
IC50: 0.3 mM
0.35
NADP+
Elizabethkingia meningoseptica
O08351
IC50: 0.35 mM
1
o-vanadate
Elizabethkingia meningoseptica
O08351
IC50: 1 mM
170
phosphate
Elizabethkingia meningoseptica
O08351
IC50: 170 mM
7
Tartrate
Elizabethkingia meningoseptica
O08351
IC50: 7 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
-
5'-dAMP
0.0055
-
pH 8, 42C
0.013
-
lysosomal enzyme
0.17
-
crude enzyme from supernatant, at pH 6.5 and 37C
0.256
-
cytosolic enzyme
1.37
-
substrate p-nitrophenyl phosphate, lysosomal enzyme
1.4
-
-
2.3
-
recombinant mutant, DELTA55 gPAPP protein
6.5
-
substrate 3'-UMP
9.5
-
recombinant gPAPP protein, full-lenght
12.6
-
substrate 5'-dTMP
35.83
-
after 211fold purification, at pH 6.5 and 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8 - 5.5
-
lysosomal enzyme
4 - 5
-
cytosolic enzyme, absence of Mg2+, substrates 3'-AMP and 3'-dAMP
5
-
lysosomal enzyme, substrate 5'-AMP
5.5 - 7.5
-
substrate-dependent
5.5
-
cytosolic enzyme, presence of Mg2+, substrate 3'-dCMP
6 - 8
-
nervous ganglia enzyme
7.2
-
digestive gland enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 7
-
lysosomal enzyme, substrate 5'-AMP
3 - 8.5
-
isozyme NSP-I
4 - 8
-
isozyme NSP-II
4.5 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
50 - 60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
25: about 70% of maximal activity, 50C: about 10% of maximal activity
25 - 41
-
activation energy in this range: 12.4 kcal/mol
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
morphological differences in the absence of functional protein
Manually annotated by BRENDA team
-
CCD-1138Sk, expression in
Manually annotated by BRENDA team
-
expression in
Manually annotated by BRENDA team
-
chondrocytes of costal cartilage and in the surrounding perichondrium, hypocellular with abnormal, fibrous-appearing structures
Manually annotated by BRENDA team
-
expression in
Manually annotated by BRENDA team
-
expression in
Manually annotated by BRENDA team
-
cerebellum, primary cell cultures of 8-day-old Wistar rats
Manually annotated by BRENDA team
wild-type, mutants
Manually annotated by BRENDA team
-
expression in
Manually annotated by BRENDA team
-
expression in
Manually annotated by BRENDA team
-
expression in
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
expression in
Manually annotated by BRENDA team
-
expression in
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
type II orientation, entire catalytic core of the gPAPP protein resides within
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
-
2 * 22000, SDS-PAGE
29000
1 * 29000, calculated from nucleotide sequence
35000
-
gel filtration
35700
-
monomeric YjjG, gel filtration
41000
-
gel filtration
41600
-
monomeric SurE, gel filtration
45000 - 50000
-
spleen, cytoplasm, gel filtration
52800
-
dimeric YjjG, gel filtration
71300
-
trimeric YfbR, gel filtration
79500
-
lysosomal enzyme, sucrose density gradient centrifugation
90000
-
SDS-PAGE
100000
-
above, tetrameric YjjG and YfbR, gel filtration
125000
-
cytosolic enzyme, gel filtration
150000
-
gel filtration
630000
-
dodecameric association of PAN-A/1
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
monomer
1 * 29000, calculated from nucleotide sequence
oligomer
-
x * 35700, YjjG, SDS-PAGE and gel filtration, x * 41600, SurE, SDS-PAGE and gel filtration
additional information
-
SurE, YfbR, and YjjG show monomeric, dimeric, trimeric, and tetrameric forms, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
7 potential N-glycosylation sites, at least one high-mannose or hybrid N-glycan in mature plasma membrane-localized protein, deglycosylation with peptide N-glycosidase
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method with 8% polyethylene glycol 4000, 0.2 M ammonium sulfate, 0.1 M sodium acetate, pH 4.8, and 10 mM CaCl2
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51
-
inactivation above
60
-
15 min, 20% loss of activity, isozymes NSP-I and NSP-II
additional information
-
serum albumin or dithiothreitol stabilizes cytosolic enzyme at 37C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes
-
the enzyme is stabilized by 2 M NaCl with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. The PAN-A/1 complex is more stable in low salt buffer with KCl compared to NaCl based on ATPase activity assay
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM Tris-HCl buffer, pH 7.5, 1 mM dithiothreitol, 2 months
-
-70C, 0.5 mg/ml bovine serum albumin, several months
-
0C, moderately stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phosphocellulose column chromatography, and UltraPak TSK G4000gel filtration
-
isozymes NSP-I, NSP-II
-
liver cytosol
-
liver lysosomes
-
Ni-NTA agarose chromatography
nickel-nitrilotriacetic acid-agarose chromatography and Sephacryl S-100 gel filtration
-
PAN-A/1 is purified to homogeneity
-
purified from baculovirus-infected cells, gel filtration
-
spleen cytosol
-
spleen, cytoplasm
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells and COS cells
-
expressed in Escherichia coli BL21(DE3) cells and COS-1 cells
-
expressed in Escherichia coli, mutants of SAL1 protein
expression in Escherichia coli
expression of NTPDase3 in COS-1 cells, pcDNA3 mammalian expression vector, co-transfection experiments, ER-targeted NTPDase3 construct generated by insertion mutagenesis, catalytically inactive G221A mutant of NTPDase3 as a control
expression of recombinant gPAPP protein using a baculovirus system, full-lenght protein and the DELTA55 gPAPP mutant, a secreted form that lacks the transmembrane domain
-
gene xapy, DNA and amino acid sequence determination and analysis, expression in HEK293 cells as functional secreted recombinant enzyme
overexpression in Saccharomyces cerevisiae as GST-fusion protein
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A287C
-
decreased activity
C257S
-
wild type-like activity
D228T
-
decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
D228T/K224N
-
largely restores the ability to form dimers and shows increased ADPase activity compared to the wild type enzyme
E130Y
-
super-active mutant
E130Y/K201M/E216M
-
shows increased activity towards ADP
E130Y/K201M/T206K/T207E/E216M
-
shows increased activity towards ADP
I170C
-
decreased activity
I170E
-
decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
I170K
-
decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
S109C
-
decreased activity
S172C
-
decreased activity
S226C
-
decreased activity
S278C
-
decreased activity
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
highly expressed in glioblastoma stem-like cells compared with normal brain and neural stem cells. Knockdown of isoform E-NPP1 in cultured glioblastoma stem-like cells results in an overall downregulation of stem cell-associated genes, induction of differentiation into astrocytic cell lineage, impairment of sphere formation, in addition to increased cell death, accumulation of cells in G1/G0 cell cycle phase and sensitisation to chemotherapeutic treatment. Knockdown of E-NPP1 affects purine and pyrimidine metabolism. E-NPP1, by acting upstream of E2F1, is indispensable for the maintenance of glioblastoma stem-like cells in vitro and hence required to keep glioblastoma stem-like cells in an undifferentiated, proliferative state