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Information on EC 3.1.3.6 - 3'-nucleotidase
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3.1.3.6 3'-nucleotidaseIUBMB Comments
Wide specificity for 3'-nucleotides.
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Word Map
- 3.1.3.6
- leishmania
- promastigotes
-
trypanosomatid
- donovani
- crithidia
- luciliae
- 3'-ribonucleotides
- 3'-nucleotides
-
purine-starved
-
sandfly
- phosphomonoesterase
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3'-nucleotidase, 3'-nucleotidase/nuclease, 3'nt/nu, 3'-n'ase, ld3'nt/nu, 3'-nt/nu, la3'-nucleotidase, ecto-3'-nucleotidase, 3'nucleotidase/nuclease, 3'-nt, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-mononucleotidase
-
-
-
-
3'-NT
3'-NT/Nu
3'-nucleotidase/nuclease
3'-phosphatase
-
-
-
-
3'-ribonucleotidase
-
-
-
-
3'NT/NU
CpdB
Deoxyribonuclease PA3
-
-
-
-
ecto 3'-nucleotidase
ecto-3'-nucleotidase
ecto-3'-nucleotidase/nuclease
Endonuclease PA3
-
-
-
-
nucleotidase, 3'-
-
-
-
-
SO3565
CpdB
the protein has 3 '-nucleotidase and 2 ',3 '-cyclic-mononucleotide phosphodiesterase activities
CpdB
-
bifunctional 2',3' cyclic nucleotide 2' phosphodiesterase/3' nucleotidase
CpdB
Shewanella oneidensis MR-1 / ATCC 700550
-
bifunctional 2',3' cyclic nucleotide 2' phosphodiesterase/3' nucleotidase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3'-ribonucleotide phosphohydrolase
Wide specificity for 3'-nucleotides.
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CAS REGISTRY NUMBER
COMMENTARY
9025-84-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-O-methyladenosine 3'-monophosphate + H2O
2'-O-methyladenosine + phosphate
-
-
-
?
3'-AMP
?
-
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
-
92% of the activity with 3'-IMP
-
?
3'-AMP + H2O
adenosine + phosphate
-
74% of the activity with 3'-IMP
-
?
3'-CMP + H2O
cytosine + phosphate
-
2% of the activity with 3'-AMP
-
?
3'-CMP + H2O
cytosine + phosphate
-
2% of the activity with 3'-AMP
-
?
3'-CMP + H2O
cytosine + phosphate
-
8% of the activity with 3'-IMP
-
?
3'-CMP + H2O
cytosine + phosphate
-
6% of the activity with 3'-IMP
-
?
3'-CMP + H2O
cytosine + phosphate
-
23.5% of the activity with 3'-AMP
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
13.3% of the activity with 3'-AMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
6% of the activity with 3'-AMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
6% of the activity with 3'-AMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
45% of the activity with 3'-AMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
21% of the activity with 3'-IMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
24% of the activity with 3'-IMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
42.2% of the activity with 3'-AMP
-
?
3'-UMP + H2O
uridine + phosphate
-
44% of the activity with 3'-AMP
-
?
3'-UMP + H2O
uridine + phosphate
-
44% of the activity with 3'-AMP
-
?
3'-UMP + H2O
uridine + phosphate
-
37% of the activity with 3'-IMP
-
?
3'-UMP + H2O
uridine + phosphate
-
59% of the activity with 3'-IMP
-
?
3'-UMP + H2O
uridine + phosphate
-
42.3% of the activity with 3'-AMP
-
?
a 3'-ribonucleotide + H2O
a ribonucleoside + phosphate
-
-
-
-
?
a 3'-ribonucleotide + H2O
a ribonucleoside + phosphate
-
-
-
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
bifunctional enzyme with 3'-nucleotidase activity and nuclease activity
-
?
additional information
?
-
-
bifunctional enzyme with 3'-nucleotidase activity and nuclease activity
-
?
additional information
?
-
the enzyme is involved in the salvage of preformed purines via the hydrolysis of either 3'-nucleotides or nucleic acids
-
?
additional information
?
-
-
the enzyme is involved in the salvage of preformed purines via the hydrolysis of either 3'-nucleotides or nucleic acids
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
the bifunctional enzyme with 3'-nucleotidase and cyclic diadenylate phosphodiesterase activities also exhibits very high efficiencies for 2 ',3 '-cyclic mononucleotides, c-di-GMP, c-di-AMP, 2',3'-cAMP and bis-4-nitrophenylphosphate
-
-
?
additional information
?
-
-
the enzyme is involved in salvage of host-derived purines, which are essential for the survival of the parasite
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
the enzyme plays a critical role in purine salvage pathway during the rapid multiplicative expansion of the parasite population within its insect vector. Starvation of the parasite for purines results in the significant up-regulation of both the 3'-nucleotidase/nuclease mRNA and enzyme activity in promastigotes, but not in amastigotes
-
?
additional information
?
-
-
the enzyme plays a critical role in purine salvage pathway during the rapid multiplicative expansion of the parasite population within its insect vector. Starvation of the parasite for purines results in the significant up-regulation of both the 3'-nucleotidase/nuclease mRNA and enzyme activity in promastigotes, but not in amastigotes
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme cleaves RNA and heat-denatured DNA endonucleolytically producing 5'-mononucleotides and shows 3'-nucleotidase activity
-
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-AMP
?
-
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
-
-
?
a 3'-ribonucleotide + H2O
a ribonucleoside + phosphate
-
-
-
-
?
a 3'-ribonucleotide + H2O
a ribonucleoside + phosphate
-
-
-
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
the enzyme is involved in the salvage of preformed purines via the hydrolysis of either 3'-nucleotides or nucleic acids
-
?
additional information
?
-
-
the enzyme is involved in the salvage of preformed purines via the hydrolysis of either 3'-nucleotides or nucleic acids
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme is involved in salvage of host-derived purines, which are essential for the survival of the parasite
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
the enzyme plays a critical role in purine salvage pathway during the rapid multiplicative expansion of the parasite population within its insect vector. Starvation of the parasite for purines results in the significant up-regulation of both the 3'-nucleotidase/nuclease mRNA and enzyme activity in promastigotes, but not in amastigotes
-
?
additional information
?
-
-
the enzyme plays a critical role in purine salvage pathway during the rapid multiplicative expansion of the parasite population within its insect vector. Starvation of the parasite for purines results in the significant up-regulation of both the 3'-nucleotidase/nuclease mRNA and enzyme activity in promastigotes, but not in amastigotes
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
additional information
?
-
-
the enzyme cleaves RNA and heat-denatured DNA endonucleolytically producing 5'-mononucleotides and shows 3'-nucleotidase activity
-
-
?
additional information
?
-
-
the enzyme must play a critical role in purine salvage of the human pathogen
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
NaCl
-
at 0.1 M, purified enzyme, 58% reduced activity after 30 min at 37°C
Ni2+
KD: 72.3 +/- 7.61 microM Ni2+ with p-nitrophenyl phosphate, KD: 29.4 +/- 3.69 microM Ni2+ with 5'-AMP
Zn2+
Co2+
KD: 46.9 +/- 5.66 microM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
Mg2+
KD: 224.7 +/- 35.1 microM Mg2+ with p-nitrophenyl phosphate, KD: 140.0 +/- 9.99 microM Mg2+ 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
Zn2+
-
2 mol Zn2+ per mol of enzyme, nuclease PA3, the Zn atoms are chelating to some of the His residues and have important roles in the enzymatic activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
copper inhibitory effects are greater at more acidic pH than at alkaline pH. The addition of enzyme substrate, adenosine 3'-monophosphate, prevents the inhibition of enzyme activity by copper. Thiol-containing compounds are able to protect. The copper chelating agent bathocuproine sulfonate restores enzyme activity after pre-treatment of the enzyme with copper. Enzymic activity is resistant to reactive oxygen species generated during oxidation reactions of ascorbate and hydrogen peroxide catalyzed by copper