Information on EC 3.1.3.6 - 3'-nucleotidase

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

EC NUMBER
COMMENTARY hide
3.1.3.6
-
RECOMMENDED NAME
GeneOntology No.
3'-nucleotidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
phosphorous acid anhydride hydrolysis
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Purine metabolism
-
-
Pyrimidine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
3'-ribonucleotide phosphohydrolase
Wide specificity for 3'-nucleotides.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-84-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
nuclease A and nuclease B, both with 3'-nucleotidase activity
-
-
Manually annotated by BRENDA team
ATTC 11745
-
-
Manually annotated by BRENDA team
ATTC 30258
-
-
Manually annotated by BRENDA team
carrot
-
-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
also acts as nuclease
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
and strain WR683
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-
Manually annotated by BRENDA team
and strain WR683
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-
Manually annotated by BRENDA team
endonuclease with 3'-nucleotidase activity
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-
Manually annotated by BRENDA team
ATCC 30220
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-
Manually annotated by BRENDA team
rye grass
-
-
Manually annotated by BRENDA team
nuclease PA1, nuclease PA2, nuclease PA3
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-
Manually annotated by BRENDA team
very low activity
-
-
Manually annotated by BRENDA team
very low activity
-
-
Manually annotated by BRENDA team
a single protein is resonsible for nuclease and 3'-nucleotidase activity
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-
Manually annotated by BRENDA team
Shewanella oneidensis MR-1 / ATCC 700550
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-
-
Manually annotated by BRENDA team
strain EATRO Lab:110 and strain MI427
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-
Manually annotated by BRENDA team
mung bean
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
(polyphosphate)n + H2O
(polyphosphate)(n-1) + phosphate
show the reaction diagram
-
-
-
-
2'-O-methyladenosine 3'-monophosphate + H2O
2'-O-methyladenosine + phosphate
show the reaction diagram
-
-
-
?
3'-AMP
?
show the reaction diagram
-
processing of exogenously available 3'-nucleotides into a form suitable for transport across the surface membrane of the parasite, which is incapable of purine biosynthesis de novo
-
-
-
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
3'-CMP + H2O
cytosine + phosphate
show the reaction diagram
3'-dAMP + H2O
deoxyadenosine + phosphate
show the reaction diagram
3'-GMP + H2O
guanosine + phosphate
show the reaction diagram
3'-IMP + H2O
inosine + phosphate
show the reaction diagram
3'-UMP + H2O
uridine + phosphate
show the reaction diagram
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
-
-
-
-
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
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acetyl-CoA + H2O
?
show the reaction diagram
-
68% of the activity with 3'-AMP
-
-
?
adenosine 3',5'-diphosphate + H2O
?
show the reaction diagram
adenosine 3'-phenylphosphonate + H2O
?
show the reaction diagram
-
-
-
-
?
CoA-SH + H2O
?
show the reaction diagram
-
53% of the activity with 3'-AMP
-
-
?
malonyl-CoA + H2O
?
show the reaction diagram
-
53% of the activity with 3'-AMP
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
poly(I) + H2O
?
show the reaction diagram
-
low activity
-
-
?
polyadenylic acid + H2O
?
show the reaction diagram
-
-
-
-
?
polycytidylic acid + H2O
?
show the reaction diagram
-
low activity
-
-
?
polyuridylic acid + H2O
?
show the reaction diagram
-
-
-
-
?
uridine 3'-phenylphosphonate + 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
3'-AMP
?
show the reaction diagram
-
processing of exogenously available 3'-nucleotides into a form suitable for transport across the surface membrane of the parasite, which is incapable of purine biosynthesis de novo
-
-
-
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
stimulation, no absolute requirement
Co2+
KD: 46.9 +/- 5.66 microM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
Mn2+
KD: 7.24 +/- 0.71 microM Mn2+ with p-nitrophenyl phosphate, KD: 2.23 +/- 0.14 micorM Mn2+ with 5'-AMP
NaCl
-
at 0.1 M, purified enzyme, 58% reduced activity after 30 min at 37C
Ni2+
KD: 72.3 +/- 7.61 microM Ni2+ with p-nitrophenyl phosphate, KD: 29.4 +/- 3.69 microM Ni2+ with 5'-AMP
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-deoxyadenosine 3'-phosphate
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8-hydroxyquinoline
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ammonium tetrathiomolybdate
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40% inhibition at 1 mM
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dithiothreitol
p-hydroxymercuribenzoate
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phosphate
Sodium citrate
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vanadate
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30% inhibition at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
monosodium glutamate
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avtivation
additional information
-
3'NT/NU is not up-regulated when parasites are cultured under purine starvation conditions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005 - 1.46
3'-AMP
0.37 - 2.2
3'-CMP
0.072
3'-GMP
-
-
0.28
3'-IMP
-
-
5
3'-UMP
-
-
0.32
5'-AMP
+/- 0.04
0.28
5'-dGMP
+/- 0.04
0.26
5'-GMP
+/- 0.05
2.49
p-nitrophenyl phosphate
+/- 0.4
0.02
Polyphosphate
+/- 0.003
additional information
additional information
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Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.84
3'-AMP
+/- 0.37
5.93
3'-CMP
+/- 0.44
4.9
5'-AMP
+/- 0.3
8.04
5'-dGMP
+/- 0.39
11
5'-GMP
+/- 0.87
3.55
p-nitrophenyl phosphate
+/- 0.16
0.05
Polyphosphate
+/- 0.005
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24.1
ATP
with 3'-AMP as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
+/- 0.01, polyphosphate
7.24
+/- 0.34, p-nitrophenyl phosphate
10
+/- 0.61, 5'-AMP
12.1
+/- 0.90, 3'-CMP
16.4
+/- 0.80, 5'-dGMP
20.1
+/- 0.76, 3'-AMP
22.4
+/- 1.78, 5'-GMP
7900
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purified enzyme, pH 8.0, 37C
additional information
-
3'-nucleotidase activity during several days of culturing at different phosphate concentrations, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
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6
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substrates 3'-GMP, 3'-CMP
6 - 6.5
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6.5
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substrates 3'-UMP, 3'-AMP
7.5
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activity of the inside of the plasma membrane
8.5
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the presence of dithiothreitol shifts the optimum to pH 6.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
activity range, profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
60 - 70
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nuclease B with 3'-nucleotidase activity
70
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nuclease A with 3'-nucleotidase activity
70 - 75
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-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
-
activity range, profile, overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the 3'-nucleotidase activity is exclusively located on the Leishmania amazonensis external surface
Manually annotated by BRENDA team
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the N-terminal signal peptide targets the enzyme into the endoplasmic reticulum
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
x * 30200 + x * 24000, SDS-PAGE
30200
-
x * 30200 + x * 24000, SDS-PAGE
32000
-
x * 32000, nuclease PA3, SDS-PAGE
34200
-
x * 34200, SDS-PAGE
35000
-
x * 35000, nuclease PA1, SDS-PAGE
36000
-
x * 36000, SDS-PAGE
38000
-
gel filtration
40000
-
x * 40000, SDS-PAGE
41670
x * 41670, calculation from nucleotide sequence
52159
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x * 52159, calculation from amino acid sequence, this protein is translated directly into an active 43000 Da protein
147000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
in solution
oligomer
at least four identical subunits in solution
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
a single N-linked glycosylation at Asn293, MW of the N-linked glycan is 1000-2000 Da, glycosylation is not required for the enzymatic function
lipoprotein
side-chain modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
-
24 h at 4C stable
95080
5 - 7
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Zn2+ protects against inactivation at pH 5.0
95088
5 - 6
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purified enzyme, 20 min, 30C, stable, 50% of maximal activity at pH 4.5 and pH 6.5, inactive below pH 4.0 and above pH 7.0, profile, overview
714527
6 - 8
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nuclease A and nuclease B, both with 3'-nucleotidase activity
95082
7 - 9
-
-
95085
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 60
-
purified enzyme, 20 min, stable, sharp drop in activity above 60C, profile, overview
50
-
20 min, 50% inactivation
60
-
stable below
80
-
15 min, 80% inactivation
83
-
30 min, pH, 7.5 60% inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.1 M NaCl, purified enzyme, 58% reduced activity after 30 min at 37C
-
dilution causes loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.01 M Tris-HCl buffer, pH 7.5, 0.3 M NaCl
-
0C, purified enzyme stable
-
4C, 0.04 M sodium acetate buffer, pH 5.5, 4 months stable
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4C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurificaction with nuclease
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copurification with nuclease
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native enzyme from fruit bodies by ammonium sulfate fractionation, and further 12fold by anion exchange and cation exchange chromatography, hydroxyapatite chromatography, and gel filtration to homogeneity
-
nuclease A and nuclease B, both with 3'-nucleotidase activity
-
nuclease PA1, nuclease PA2, nuclease PA3
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Sephadex G-25 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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