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(polyphosphate)n + H2O
(polyphosphate)(n-1) + phosphate
-
-
-
?
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
3'-CMP + H2O
cytosine + phosphate
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
3'-GMP + H2O
guanosine + phosphate
3'-IMP + H2O
inosine + phosphate
3'-UMP + H2O
uridine + phosphate
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
-
-
?
a 3'-ribonucleotide + H2O
a ribonucleoside + phosphate
acetyl-CoA + H2O
?
-
68% of the activity with 3'-AMP
-
-
?
adenosine 3',5'-diphosphate + H2O
?
adenosine 3'-phenylphosphonate + H2O
?
-
-
-
-
?
CoA-SH + H2O
?
-
53% of the activity with 3'-AMP
-
-
?
malonyl-CoA + H2O
?
-
53% of the activity with 3'-AMP
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
poly(I) + H2O
?
-
low activity
-
-
?
polyadenylic acid + H2O
?
-
-
-
-
?
polycytidylic acid + H2O
?
-
low activity
-
-
?
polyuridylic acid + H2O
?
-
-
-
-
?
uridine 3'-phenylphosphonate + H2O
?
-
-
-
-
?
additional information
?
-
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
highly efficient substrate
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
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'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
-
-
?
3'-CMP + H2O
cytosine + phosphate
-
-
-
?
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
-
-
-
?
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
-
-
-
?
3'-CMP + H2O
cytosine + phosphate
-
-
-
?
3'-CMP + H2O
cytosine + phosphate
-
23.5% of the activity with 3'-AMP
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
-
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
-
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
13.3% of the activity with 3'-AMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
-
-
?
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
-
29% of the activity with 3'-AMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
45% of the activity with 3'-AMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
-
-
?
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
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
-
42.2% of the activity with 3'-AMP
-
?
3'-IMP + H2O
inosine + phosphate
-
best substrate
-
?
3'-IMP + H2O
inosine + phosphate
-
best substrate
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
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
-
-
-
?
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
-
-
-
?
3'-UMP + H2O
uridine + phosphate
-
-
-
?
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
-
-
-
-
?
a 3'-ribonucleotide + H2O
a ribonucleoside + phosphate
-
-
-
-
?
adenosine 3',5'-diphosphate + H2O
?
-
-
-
-
?
adenosine 3',5'-diphosphate + H2O
?
-
-
-
-
?
adenosine 3',5'-diphosphate + H2O
?
-
83% of the activity with 3'-AMP
-
-
?
adenosine 3',5'-diphosphate + H2O
?
-
-
-
-
?
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
?
-
-
no hydrolysis of 5'-AMP
-
-
?
additional information
?
-
-
no hydrolysis of 5'-AMP
-
-
?
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
-
?
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Brown, P.H.; Ho, T.D.
Biochemical properties and hormonal regulation of barley nuclease
Eur. J. Biochem.
168
357-364
1987
Hordeum vulgare
brenda
Naseem, I.; Hadi, S.M.
Single-strand-specific nuclease of pea seeds: glycoprotein nature and associated nucleotidase activity
Arch. Biochem. Biophys.
255
437-445
1987
Pisum sativum
brenda
Nguyen, T.T.; Palcic, M.M.; Hadziyev, D.
High-performance liquid chromatographic assay of potato tuber 3'-nucleotidase
J. Chromatogr.
391
257-265
1987
Solanum tuberosum
-
brenda
Brown P.H.; Ho, T.D.
Barley aleurone layers secrete a nuclease in response to gibberellic acid. Purification and partial characterization of the associated ribonuclease, deoxyribonuclease and 3'-nucleotidase activities
Plant Physiol.
82
801-806
1986
Hordeum vulgare
brenda
Hinderer, W.; Seitz, H.U.
In vitro inhibition of carrot chalcone synthase by 3'-nucleotidase: the role of the 3-phosphate group of malonyl-coenzyme A in flavonoid biosynthesis
Arch. Biochem. Biophys.
246
217-224
1986
Daucus carota, Lolium multiflorum
brenda
Kurosawa, S.; Katoh, K.; Yokomichi, H.
Separation and characterization of alkaline nuclease in the fruit body of Flammulina velutipes
Agric. Biol. Chem.
49
2181-2183
1985
Flammulina velutipes
-
brenda
Gottlieb, M.
Enzyme regulation in a trypanosomatid: effect of purine starvation on levels of 3-nucleotidase activity
Science
227
72-74
1985
Crithidia fasciculata, Crithidia fasciculata ATTC 11745
brenda
Imagawa, H.; Toryu, H.; Ozawa, T.; Takino, Y.
Purification and characterization of nucleases from tea leaves
Agric. Biol. Chem.
46
1261-1269
1982
Camellia sinensis
-
brenda
Hecht, S.M.; Hawrelak, S.D.
Hydrolysis of ribonucleoside 3-diphosphates by rye grass 3'-nucleotidase
Biochemistry
14
974-980
1975
Lolium multiflorum
brenda
Suno, M.; Nomura, A.; Mizuno, Y.
Studies on 3-nucleotidase-nuclease from potato tubers. II. Further studies on substrate specificity and mode of action
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73
1291-1297
1973
Solanum tuberosum
brenda
Nomura, A.; Suno, M.; Mizuno, Y.
Studies on 3'-nucleotidase-nuclease from potato tubers. I. Purification and some properties of the enzyme
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70
993-1001
1971
Solanum tuberosum
brenda
Debrabant, A.; Gottlieb, M.; Dwyer, D.M.
Isoaltion and chacterization of the gene encoding the surface membrane 3'-nucleotidase/nuclease of Leishmania donovani
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71
51-63
1995
Leishmania donovani
brenda
Gbenle, G.O.; Dwyer, D.M.
Purification and properties of 3'-nucleotidase of Leishmania donovani
Biochem. J.
285
41-46
1992
Leishmania donovani
brenda
Neubert, T.A.; Gottlieb, M.
An inducible 3'-nucleotidase/nuclease from the trypanosomatid Crithidia luciliae. Purification and characterization
J. Biol. Chem.
265
7236-7242
1990
Crithidia luciliae, Crithidia luciliae ATTC 30258
brenda
Gbenle, G.O.
Characterization of a filtrable 3'-nucleotidase of Leishmania donovani
Biochim. Biophys. Acta
1203
162-167
1993
Leishmania donovani
brenda
Uchida, H.; Wu, Y.D.; Sonoda, S.; Fukushima, S.; Fukuda, J.; Takahashi, I.; Maeda, S.; Nomura, A.
Substrate properties of adenosine- and uridine-3'-phenylphosphonates for 3'-nucleotidase/nucleases
Nucleosides Nucleotides
15
649-654
1996
Vigna radiata
-
brenda
Campbell, T.A.; Zlotnick, G.W.; Neubert, T.A.; Sacci, J.B.; Gottlieb, M.
Purification and characterization of 3'-nucleotidase/nuclease from promastigotes of Leishmania donovani
Mol. Biochem. Parasitol.
47
109-117
1991
Leishmania donovani
brenda
Shimada, H.; Inokuchi, N.; Koyama, T.; Irie, M.
Purification and characterization of a nuclease from Lentinus edodes
Chem. Pharm. Bull.
39
2633-2637
1991
Lentinula edodes
brenda
Kazama, H.; Tabat, N.; Ohgi, K.; Irie, M.
Purification and chacterization of a nuclease (3'-nucleotidase) from Penicillium sp.
Chem. Pharm. Bull.
38
3081-3085
1990
Penicillium sp.
brenda
Alleman, M.M.; Gottlieb, M.
Crithidia lucilliae: starvation for purines and/or phosphate leads to the enhanced surface expression of a protein responsible for 3'-nucleotidase/nuclease activity
Exp. Parasitol.
71
146-157
1990
Crithidia luciliae
brenda
Sopwith, W.F.; Debrabant, A.; Yamage, M.; Dwyer, D.M.; Bates, P.A.
Developmentally regulated expression of a cell surface class I nuclease in Leishmania mexicana
Int. J. Parasitol.
32
449-459
2002
Leishmania mexicana (Q9GNZ4), Leishmania mexicana
brenda
Debrabant, A.; Ghedin, E.; Dwyer, D.M.
Dissection of the functional domains of the Leishmania surface membrane 3'-nucleotidase/nuclease, a unique member of the class I nuclease family
J. Biol. Chem.
275
16366-16372
2000
Leishmania donovani
brenda
Yamage, M.; Debrabant, A.; Dwyer, D.M.
Molecular characterization of a hyperinducible, surface membrane-anchored, class I nuclease of a trypanosomatid parasite
J. Biol. Chem.
275
36369-36379
2000
Crithidia luciliae (Q9NJI3), Crithidia luciliae
brenda
Debrabant, A.; Bastien, P.; Dwyer, D.M.
A unique surface membrane anchored purine-salvage enzyme is conserved among a group of primitive eukaryotic human pathogens
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220
109-116
2001
Crithidia fasciculata, Crithidia luciliae, Leishmania donovani, Leishmania infantum, Leishmania major, Leishmania mexicana, Leishmania tropica, Leptomonas seymouri, Trypanosoma brucei, Phytomonas serpens, Leishmania mexicana M379, Leishmania infantum FVM1001JL, Leishmania tropica WR664, Phytomonas serpens TCC/USP
brenda
Proudfoot, M.; Kuznetsova, E.; Brown, G.; Rao, N.N.; Kitagawa, M.; Mori, H.; Savchenko, A.; Yakunin, A.F.
General Enzymatic Screens Identify Three New Nucleotidases in Escherichia coli. Biochemical Characterization of SurE, YfbR, and Yjjg
J. Biol. Chem.
279
54687-54694
2004
Escherichia coli (P0A840)
brenda
Yin, Y.; Shimano, F.; Ashihara, H.
Involvement of rapid nucleotide synthesis in recovery from phosphate starvation of Catharanthus roseus cells
J. Exp. Bot.
58
1025-1033
2007
Catharanthus roseus
brenda
Pinchuk, G.E.; Ammons, C.; Culley, D.E.; Li, S.W.; McLean, J.S.; Romine, M.F.; Nealson, K.H.; Fredrickson, J.K.; Beliaev, A.S.
Utilization of DNA as a sole source of phosphorus, carbon, and energy by Shewanella spp.: ecological and physiological implications for dissimilatory metal reduction
Appl. Environ. Microbiol.
74
1198-1208
2008
Shewanella oneidensis, Shewanella oneidensis MR-1 / ATCC 700550
brenda
Lakhal-Naouar, I.; Ben Achour-Chenik, Y.; Boublik, Y.; Meddeb, M.; Aamouri, A.; Fattoum, A.; Louzir, H.; Chenik, M.
Identification and characterization of a new Leishmania major specific 3'nucleotidase/nuclease protein
Biochem. Biophys. Res. Commun.
375
54-58
2008
Leishmania major
brenda
Peres-Sampaio, C.E.; de Almeida-Amaral, E.E.; Giarola, N.L.; Meyer-Fernandes, J.R.
Leishmania amazonensis: effects of heat shock on ecto-ATPase activity
Exp. Parasitol.
119
135-143
2008
Leishmania amazonensis, Leishmania amazonensis MHOM/BR/75/Josefa
brenda
Hatakeyama, T.; Mizuno, K.; Kurosawa, S.
Purification and properties of a nuclease from the fruit body of Tricholoma matsutake
Biosci. Biotechnol. Biochem.
74
206-208
2010
Tricholoma matsutake
brenda
Vieira, D.P.; Paletta-Silva, R.; Saraiva, E.M.; Lopes, A.H.; Meyer-Fernandes, J.R.
Leishmania chagasi: an ecto-3'-nucleotidase activity modulated by inorganic phosphate and its possible involvement in parasite-macrophage interaction
Exp. Parasitol.
127
702-707
2011
Leishmania chagasi, Leishmania chagasi MHOM/BR/1974/PP75
brenda
Paletta-Silva, R.; Vieira, D.P.; Vieira-Bernardo, R.; Majerowicz, D.; Gondim, K.C.; Vannier-Santos, M.A.; Lopes, A.H.; Meyer-Fernandes, J.R.
Leishmania amazonensis: Characterization of an ecto-3'-nucleotidase activity and its possible role in virulence
Exp. Parasitol.
129
277-283
2011
Leishmania amazonensis
brenda
Paletta-Silva, R.; Vieira-Bernardo, R.; Cosentino-Gomes, D.; Meyer-Fernandes, J.R.
Leishmania amazonensis: inhibition of 3'-nucleotidase activity by Cu2+ ions
Exp. Parasitol.
131
63-68
2012
Leishmania amazonensis (F6MDM5), Leishmania amazonensis
brenda
Guimaraes-Costa, A.B.; DeSouza-Vieira, T.S.; Paletta-Silva, R.; Freitas-Mesquita, A.L.; Meyer-Fernandes, J.R.; Saraiva, E.M.
3-nucleotidase/nuclease activity allows Leishmania parasites to escape killing by neutrophil extracellular traps
Infect. Immun.
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1732-1740
2014
Leishmania infantum
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Freitas-Mesquita, A.L.; Gomes, M.T.; Vieira, D.P.; Paes-Vieira, L.; Nascimento, M.T.; Lopes, A.H.; Meyer-Fernandes, J.R.
Inhibitory effects promoted by 5'-nucleotides on the ecto-3'-nucleotidase activity of Leishmania amazonensis
Exp. Parasitol.
169
111-118
2016
Leishmania amazonensis, Leishmania amazonensis MHOM/BR/75/Josefa
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Freitas-Mesquita, A.L.; Meyer-Fernandes, J.R.
3'nucleotidase/nuclease in protozoan parasites Molecular and biochemical properties and physiological roles
Exp. Parasitol.
179
1-6
2017
Crithidia sp., Leishmania amazonensis
brenda
Lopez-Villamizar, I.; Cabezas, A.; Pinto, R.; Canales, J.; Ribeiro, J.; Cameselle, J.; Costas, M.
The characterization of Escherichia coli CpdB as a recombinant protein reveals that, besides having the expected 3'-nucleotidase and 2,3-cyclic mononucleotide phosphodiesterase activities, it is also active as cyclic dinucleotide phosphodiesterase
PLoS ONE
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e0148508
2016
Escherichia coli (P08331)
brenda