HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 3.1.3.5 - 5'-nucleotidase
for references in articles please use BRENDA:EC3.1.3.5
Word Map on EC 3.1.3.5
- 3.1.3.5
- nucleoside
- deaminase
- adp
- lymphocyte
- triphosphate
- vesicles
- pyrimidine
- endothelial
- erythrocyte
- phosphodiesterase
- adenylate
-
histochemical
-
purinergic
- inosine
- na+
-
phosphorylase
- ntpdases
- lysosome
-
diphosphohydrolase
- ectonucleotidases
- 5'-monophosphate
-
cytochemical
- glucose-6-phosphatase
- platelet
-
synaptosomes
-
concanavalin
- 5'-diphosphate
- acetylcholinesterase
-
histochemistry
- hypoxanthine
-
k+-atpase
- lymphatic
- mg2+-atpase
-
ecto-enzymes
- adpase
- sarcolemma
- dipyridamole
- apyrase
- ecto-atpase
- deoxycytidine
-
plasma-membrane
-
enzyme-histochemical
-
diphosphatase
-
canalicular
-
ouabain-sensitive
-
phosphomonoesterase
- ehna
- dpcpx
- deoxycoformycin
- pharmacology
- nutrition
- medicine
- hgprt
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
3.1.3.5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
5'-nucleotidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
-
-
-
-
a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
conserved motif I is involved in formation and stabilization of the covalent enzyme-phosphate intermediate. T249 and K292 in motif II contribute to stabilize the enzyme-phospho adduct. D351 and D356 in motif III coordinate the magnesium ion required for catalysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric esters
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
5'-ribonucleotide phosphohydrolase
Wide specificity for 5'-nucleotides.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9027-73-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme has both Mg2+-dependent diphosphohydrolyse/apyrase and 5’-nucleotidase activity
SwissProt
-
649279, 649280, 650722, 652372, 677295, 677542, 678418, 679669, 680780, 681753, 682200, 682217, 690362, 691078, 691082, 692002, 692592, 693298, 693385, 694133, 694138, 708161, 709210, 728860, 730020, 736041, 95024, 95025, 95035, 95062, 95064, 95073
-
-
isoform cytosolic 5'-nucleotidase II, expression in Escherichia coli
SwissProt
patients with acute lymphoblastic leukemia during 6-mercaptopurine treatment
-
-
-
652980, 679250, 680180, 681194, 681729, 691839, 692268, 692272, 692462, 707006, 708043, 709642, 710220, 710524, 715146, 95052, 95074
-
-
-
649524, 651540, 665608, 677490, 677509, 677542, 678104, 679085, 679669, 680226, 681724, 681894, 681897, 682113, 682115, 691398, 692192, 693953, 694138, 696924, 707133, 707925, 708576, 709460, 709469, 710524, 715146, 715987, 95029, 95040, 95041, 95042, 95045, 95049, 95050, 95053, 95056, 95057, 95066, 95067, 95068, 95069, 95070
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
cytosolic 5'-nucleotidase cN-II is implicated in drug resistance in patients and dephosphorylates 5-fluoro-dUMP, 3'-azido-3-dTMP, 2'-chloro-2'-deoxyAMP, and related compounds, which represent the monophosphorylated forms of nucleoside prodrugs
metabolism
physiological function
additional information
metabolism
-
the key and rate-limiting enzyme in the ectonucleotidase pathway is ecto-5'-nucleotidase, which catalyzes the final step of dephosphorylation of AMP to adenosine
metabolism
-
5'-nucleotidases are involved in the purine and pyrimidine nucleotide metabolic pathways, overview. CD73 enzymatic activity is implicated in two major extracellular metabolic pathways with distinct physiological roles, extracellular adenosine nucleotide and NAD+ metabolism
metabolism
-
Trichomonas foetus is devoid of the ability to synthesize purine nucleotides de novo, depending instead on salvaging purines from the host environment. Ecto-5'-nucleotidase catalyzes the final step of extracellular nucleotide degradation, the hydrolysis of nucleoside 5'-monophosphates to the corresponding nucleosides and phosphate
metabolism
-
the key and rate-limiting enzyme in the ectonucleotidase pathway is ecto-5'-nucleotidase, which catalyzes the final step of dephosphorylation of AMP to adenosine
-
physiological function
-
the ecto-5'-nucleotidase plays a role in the control of extracellular nucleotide concentrations in the cell and is involved in the release of free adenosine into extracellular medium
physiological function
-
the enzyme plays a role in the generation of extracellular adenosine, a key modulator of male fertility
physiological function
-
the enzyme plays a role in the generation of extracellular adenosine, a key modulator of male fertility
physiological function
-
cytosolic 5'-nucleotidase II catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates and participates in the regulation of purine nucleotide pools within the cell
physiological function
-
5'-nucleotidase UshA is required for growth when nucleotides are provided as the sole source of phosphate, a condition that is likely relevant to bacterial growth in the wild
physiological function
-
5'-nucleotidase activities regulate the quantity of nucleotides generated from both de novo and salvage pathways, overview. 5'-Nucleotidase designates a set of enzymes, which catalyze the hydrolysis of ribonucleoside and deoxyribonucleoside monophosphates into the corresponding nucleosides plus phosphate. 5'-Nucleotidases are classified according to subcellular localization, nucleobase specificity and their ability to hydrolyze deoxynucleoside monophosphate substrates. Membrane-bound 5'-nucleotidases are ectoenzymes principally involved in salvage of extracellular nucleosides, and often display a preference toward adenosine monophosphate, thereby modulating signal transduction cascades involving purinergic receptors. Cytosolic 5'-nucleotidases are members of the haloacid dehalogenase superfamily of enzymes, which are two-domain proteins containing a modified Rossman fold as the core and a variable cap structure. Extracellular and intracellular 5'-nucleotidase activities participate in purine and pyrimidine salvage to support balanced synthesis of nucleotides, which is critical for maintaining high fidelity DNA replication. The major physiological roles for CD73 in extracellular adenosine metabolism are severalfold, overview. cNII is subject to complex allosteric regulation
physiological function
-
ISN1 is responsible for virtually all IMP 5'-nucleotidase activity in budding yeast cells and is required for cells to release inosine into the culture medium
physiological function
-
upon blockade of enzyme by concanavalin A, the strength of adhesion to different extracellular matrix proteins is not altered, but at the same time the invasion ability of the cells is decreased. Knocking down the enzyme in melanoma cells does not influence cell invasion but abolishes their migration on tenascin C, indicating that an enzyme-tenascin C complex is involved in cell migration and invasion and thus in the regulation of melanoma progression
physiological function
-
the two domains can be expressed individually in Escherichia coli and fold independently. The C-terminal domain, which contains the substrate-binding pocket, is completely inactive while the N-terminal domain with the two-metal-ion-centers and the core catalytic residues exhibits significant activity, especially towards substrates with activated phosphate bonds such as ATP, ADP, 4-nitrophenyl phosphate. The two domains do not reconstitute the full-length protein from the two folded individual domains
physiological function
transgenic mice expressing a dominant active mutant of downstream regulatory element antagonist modulator, daDREAM, show a drastic reduction of the amount of transcript of Ca2+-activated nucleotidase. Ca2+-activated nucleotidase down-regulation is also found in neuroblastoma SH-SY5Y cells stably overexpressing wild type DREAM or daDREAM, thus providing a simple cell model to investigate the protein maturation pathway. The down-regulation of CANT1 is associated with reduced protein secretion and increased degradation rates
physiological function
-
in neonatal blood plasma, soluble 5'-nucleotidase and alkaline phosphatase mediate conversion of AMP to adenosine, whereas soluble adenosine deaminase catabolizes adenosine to inosine. Newborn blood plasma demonstrates substantially higher adenosine-generating 5'-nucleotidase and alkaline phosphatase activity and lower metabolizing adenosine deaminase activity than adult plasma. Supplementation with AMP inhibits whereas selective pharmacologic inhibition of 5'-nucleotidase enhances Toll-like receptor-mediated tumor necrosis factor TNF-alpha production in neonatal whole blood
physiological function
-
the ecto-5'-nucleotidase plays a role in the control of extracellular nucleotide concentrations in the cell and is involved in the release of free adenosine into extracellular medium
-
physiological function
-
the enzyme plays a role in the generation of extracellular adenosine, a key modulator of male fertility
-
additional information
-
the enzyme interferes with the phosphorylation-dependent activation of nucleoside analogues used in the treatment of cancer and viral diseases
additional information
-
unilateral cortical stab injury causes a rapid and irreversible loss of the enzyme from neurons, accounting for a decrease in the overall enzyme expression, accompanied with a gradual increase in e-5NT-positive astrocytes, accounting for upregulation of the enzyme levels in the injured area. CSI induces dynamic changes in the expression pattern of e-5NT that modify the ATP/adenosine ratio and the extent of P1 and P2 receptors activation and, therefore, outcome of the pathological processes after cortical stab injury
additional information
-
CD73 is highly induced by ischemia and hypoxia, and increased expression in cardiac ischemia is mediated by a positive feedback loop involving adenosine
additional information
-
unilateral cortical stab injury causes a rapid and irreversible loss of the enzyme from neurons, accounting for a decrease in the overall enzyme expression, accompanied with a gradual increase in e-5NT-positive astrocytes, accounting for upregulation of the enzyme levels in the injured area. CSI induces dynamic changes in the expression pattern of e-5NT that modify the ATP/adenosine ratio and the extent of P1 and P2 receptors activation and, therefore, outcome of the pathological processes after cortical stab injury
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(polyphosphate)n + H2O
(polyphosphate)n-1 + phosphate
-
-
-
-
1,N6-ethenoadenosine 5'-phosphate + H2O
1,N6-ethenoadenosine ribonucleoside + phosphate
-
45% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
1-glycerophosphate + H2O
glycerol + phosphate
-
1% of the activity with 5’-IMP
-
-
?
2'-chloro-2'-deoxyAMP + H2O
2'-chloro-2'-deoxyadenosine + phosphate
-
cNII
-
-
?
2-(cyclohexylethylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylethylthio)adenosine + phosphate
-
-
-
-
?
2-(cyclohexylmethylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylmethylthio)adenosine + phosphate
-
-
-
-
?
2-(cyclohexylthio)adenosine 5'-monophosphate + H2O
2-(cyclohexylthio)adenosine + phosphate
-
-
-
-
?
2-(cyclopentylthio)adenosine 5'-monophosphate + H2O
2-(cyclopentylthio)adenosine + phosphate
-
-
-
-
?
2-(dioxanylethylthio)adenosine 5'-monophosphate + H2O
2-(dioxanylethylthio)adenosine + phosphate
-
-
-
-
?
2-(dioxolanylethylthio)adenosine 5'-monophosphate + H2O
2-(dioxolanylethylthio)adenosine + phosphate
-
-
-
-
?
2-(hexylthio)adenosine 5'-monophosphate + H2O
2-(hexylthio)adenosine + phosphate
-
-
-
-
?
2-(propylthio)adenosine 5'-monophosphate + H2O
2-(propylthio)adenosine + phosphate
-
-
-
-
?
2-chloro-2'-deoxyadenosine monophosphate + H2O
2-chloro-2'-deoxyadenosine + phosphate
39% of the activity with 5'-AMP
-
?
3'-IMP + H2O
inosine + phosphate
-
1% of the activity with 5'-IMP
-
?
3-beta-ribofuranosyladenine 5'-monophosphate + H2O
3-beta-ribofuranosyladenine + phosphate
-
24% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferol + phosphate
-
-
?
5'-dUMP + H2O
deoxyuridne + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
6-chloropurine ribonucleoside 5'-monophosphate + H2O
6-chloropurine ribonucleoside + phosphate
-
50% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
9-beta-D-arabinosyl-2-fluoroadenine monophosphate + H2O
9-beta-D-arabinosyl-2-fluoroadenine + phosphate
-
-
-
-
?
adenosine 5'-O-thiophosphate + H2O
?
-
6% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
-
?
dAMP + H2O
deoxyadenosine + phosphate
91% of the activity with 5'-AMP
-
?
dGMP + H2O
deoxyguanosine + phosphate
75% of the activity with 5'-AMP
-
?
dTMP + H2O
deoxythymidine + phosphate
-
7.5% of the activity with 5'-IMP
-
?
dUMP + H2O
deoxyuridine + phosphate
7% of the activity with 5'-AMP
-
?
p-nitrophenylphosphate + H2O
p-nitrophenol + phosphate
-
plasma membrane enzyme: 1% of the activity with 5'-AMP, Golgi apparatus enzyme: 39% of the activity with 5'-AMP
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
about 55% of the activity with 4-methylumbelliferyl phosphate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
5'-AMP + H2O
?
-
enzyme in the system for the hydrolysis of extracellular nucleotides so that product nucleosides are readily transported into the cell
-
-
-
5'-AMP + H2O
?
-
the enzyme is responsible for the production of adenosine in the cardiac tissue
-
-
-
5'-AMP + H2O
adenosine + phosphate
-
best substrate for enzyme from plasma membrane and Golgi apparatus
-
?
5'-AMP + H2O
adenosine + phosphate
-
highly specific, no hydrolysis of other nucleotides
-
?
5'-AMP + H2O
adenosine + phosphate
-
highly specific, no hydrolysis of other nucleotides
-
?
5'-AMP + H2O
adenosine + phosphate
-
absence of ADP, 60% loss of activity
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
17% of the activity with 5’-IMP
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
101% of the activity of 5'-IMP
-
?
5'-AMP + H2O
adenosine + phosphate
about 35% of the activity with 4-methylumbelliferyl phosphate
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
preferred substrate for cNI and eNs
-
?
5'-AMP + H2O
adenosine + phosphate
-
enzyme is responsible for generation of adenosine from AMP. Adenosine is involved in a number of cardioprotective mechanisms. TNF-alpha may reduce the capacity of human endothelial cels to produce adenosine by a decrease in activity of ecto-5'-nucleotidase. The loss of ecto-5'-nucleotidase may lead to decreased production of anti-inflammatory adenosine and retention of proinflammatory nucleotides
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
36.3% of the activity with 5'-IMP
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
664550, 677490, 677509, 678104, 679085, 679669, 681724, 681894, 681897, 682113, 682115, 691398, 692192, 693953, 694138, 715146, 715987
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
64% of the activity of ATP
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
30% of the activity with 5’-IMP
-
-
?
5'-AMP + H2O
adenosine + phosphate
enzyme is monospecific for AMP among nucleoside 5’-monophosphates
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
23.1% of the activity with 5'-AMP
-
?
5'-CMP + H2O
cytidine + phosphate
-
125% of the activity with 5'-AMP
-
?
5'-CMP + H2O
cytidine + phosphate
-
21% of the activity with 5’-IMP
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
85% of the activity of 5'-IMP
-
?
5'-CMP + H2O
cytidine + phosphate
about 30% of the activity with 4-methylumbelliferyl phosphate
-
?
5'-CMP + H2O
cytidine + phosphate
85% of the activity with 5'-AMP
-
?
5'-CMP + H2O
cytidine + phosphate
-
56.2% of the activity with 5'-AMP
-
?
5'-CMP + H2O
cytidine + phosphate
-
18.4% of the activity with 5'-IMP
-
?
5'-CMP + H2O
cytidine + phosphate
-
87% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-CMP + H2O
cytidine + phosphate
-
65% of the activity with 5'-AMP, brain cytosolic enzyme
-
?
5'-CMP + H2O
cytidine + phosphate
-
36% dephosphorylation in relation to AMP
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
93% of the activity with 5'-AMP
-
?
5'-CMP + H2O
cytidine + phosphate
-
87% activity compared to 5'-AMP
-
-
?
5'-CMP + H2O
cytidine + phosphate
-
87% activity compared to 5'-AMP
-
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
19.7% of the activity with 5'-AMP
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
Bacillus sp. (in: Bacteria) No. A-59
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
Bacillus sp. (in: Bacteria) No. A-59
-
19.7% of the activity with 5'-AMP
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
22% of the activity with 5'-AMP
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
66% of the activity with 5'-AMP
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
presence of ADP, 66% of the activity with 5’-AMP
-
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
53% of the activity of 5'-IMP
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
54% of the activity with 5'-AMP
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
20% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
7% of the activity with 5'-AMP, brain cytosolic enzyme
-
-
-
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
14% of the activity with 5'-AMP
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
presence of ADP, 16% of the activity with 5’-AMP
-
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytosine 5'-phosphate
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytosine 5'-phosphate
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytosine 5'-phosphate
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytosine 5'-phosphate
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
28% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
49.9% of the activity with 5'-AMP
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
35% of the activity with 5'-AMP
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
60.9% of the activity with 5'-AMP
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
102% of the activity with 5’-IMP
-
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
23% of the activity with 5'-IMP, cytoplasmic enzyme
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
95% of the activity with 5’-IMP
-
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
99% of the activity with 5’-IMP
-
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
7.1% of the activity with 5’-IMP
-
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
55% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
17.5% of the activity with 5’-IMP
-
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
10% of the activity with 5’-IMP
-
-
?
5'-GMP + H2O
guanidine + phosphate
-
57% dephosphorylation in relation to AMP
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
plasma membrane enzyme: 2.85% of the activity with 5'-AMP, Golgi apparatus enzyme: 46% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
16.7% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
Bacillus sp. (in: Bacteria) No. A-59
-
16.7% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
117% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
33.5% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
89% of the activity with 5’-IMP
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
52% of the activity of 5'-IMP
-
?
5'-GMP + H2O
guanosine + phosphate
about 30% of the activity with 4-methylumbelliferyl phosphate
-
?
5'-GMP + H2O
guanosine + phosphate
-
85% of the activity with 5'-IMP, cytoplasmic enzyme
-
?
5'-GMP + H2O
guanosine + phosphate
57% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
53.6% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
preferred substrate. Substrate GMP acting as an activator, partitioning between the allosteric and active site, is the basis for the sigmoidicity of the initial velocity versus GMP concentration plot
-
-
?
5'-GMP + H2O
guanosine + phosphate
preferred substrate. Substrate GMP acting as an activator, partitioning between the allosteric and active site, is the basis for the sigmoidicity of the initial velocity versus GMP concentration plot
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
97.6% of the activity with 5'-IMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
50% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-GMP + H2O
guanosine + phosphate
-
19% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
67% of the activity of ATP
-
?
5'-GMP + H2O
guanosine + phosphate
-
99% of the activity with 5’-IMP
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
52% of the activity with 5'-AMP
-
?
5'-GMP + H2O
guanosine + phosphate
-
68% activity compared to 5'-AMP
-
-
?
5'-GMP + H2O
guanosine + phosphate
-
68% activity compared to 5'-AMP
-
-
?
5'-IMP + H2O
?
-
the enzyme is principally responsible for dephosphorylation of 5'-IMP but may have some role in adenosine formation
-
-
-
5'-IMP + H2O
deoxyinosine + phosphate
-
presence of ADP, 38% of the activity with 5’-AMP
-
-
?
5'-IMP + H2O
deoxyinosine + phosphate
61% of the activity with 5'-AMP
-
?
5'-IMP + H2O
inosine + phosphate
-
preferred substrate of cytosolic thymus enzyme
-
-
?
5'-IMP + H2O
inosine + phosphate
-
36% of the activity with 5'-AMP, brain cytosolic enzyme
-
-
?
5'-IMP + H2O
inosine + phosphate
-
55% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
-
?
5'-IMP + H2O
inosine + phosphate
-
63% of the activity with 5'-AMP
-
?
5'-TMP + H2O
thymidine + phosphate
-
7.4% of the activity with 5'-AMP
-
?
5'-TMP + H2O
thymidine + phosphate
about 15% of the activity with 4-methylumbelliferyl phosphate
-
?
5'-TMP + H2O
thymidine + phosphate
13% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
-
plasma membrane enzyme: 7.5% of the activity with 5'-AMP, Golgi apparatus enzyme: 16.2% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
-
10.6% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
Bacillus sp. (in: Bacteria) No. A-59
-
10.6% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
-
41% of the activity with 5’-IMP
-
-
?
5'-UMP + H2O
uridine + phosphate
-
120% of the activity of 5'-IMP
-
?
5'-UMP + H2O
uridine + phosphate
about 30% of the activity with 4-methylumbelliferyl phosphate
-
?
5'-UMP + H2O
uridine + phosphate
-
14% of the activity with 5'-IMP, cytoplasmic enzyme
-
?
5'-UMP + H2O
uridine + phosphate
78% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
-
33.3% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
-
180% of the activity with 5'-AMP, preferred substrate
-
?
5'-UMP + H2O
uridine + phosphate
-
52.3% of the activity with 5'-IMP
-
?
5'-UMP + H2O
uridine + phosphate
-
93% of the activity with 5'-AMP, heart, membrane-bound enzyme
-
?
5'-UMP + H2O
uridine + phosphate
-
111% of the activity with 5'-AMP, brain cytosolic enzyme
-
?
5'-UMP + H2O
uridine + phosphate
-
51% dephosphorylation in relation to AMP
-
-
?
5'-UMP + H2O
uridine + phosphate
-
83% of the activity of ATP
-
?
5'-UMP + H2O
uridine + phosphate
-
80% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
-
60% activity compared to 5'-AMP
-
-
?
5'-UMP + H2O
uridine + phosphate
-
60% activity compared to 5'-AMP
-
-
?
5'-XMP + H2O
xanthosine + phosphate
-
23% of the activity with 5'-IMP, cytoplasmic enzyme
-
?
ADP + 2 H2O
adenosine + 2 phosphate
-
114% of the activity of ATP
-
-
?
ADP + H2O
adenosine + diphosphate
-
9.6% of the activity with 5'-AMP
-
?
ADP + H2O
adenosine + diphosphate
-
4.5% of the activity with 5'-AMP
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
dCMP + H2O
deoxycytidine + phosphate
10% of the activity with 5'-AMP
-
?
dIMP + H2O
deoxyinosine + phosphate
84% of the activity with 5'-AMP
-
?
dIMP + H2O
deoxyinosine + phosphate
-
103% of the activity with 5'-IMP
-
?
diphosphate + H2O
2 phosphate
-
5.8% activity compared to 5'-AMP
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
additional information
?
-
-
significant differences in substrate specificity between the isoforms are interpreted in terms of variable glycosylation causing steric hindrance of the substrate-binding site
-
?
additional information
?
-
-
the enzyme acts through the formation of a phosphoenzyme intermediate, essential role of Asp52 in the catalytic machinery, Asp54 assists in the formation of the acyl phosphate species
-
?
additional information
?
-
-
the soluble forms of enzyme in seminal plasma have a putative role in signalling interactions with spermatozoa following ejaculation and capacitations in the female reproductive tract
-
?
additional information
?
-
-
no substrate: 3'-IMP, 1-glycerophosphate
-
-
-
additional information
?
-
-
bifunctional enzyme with UDP-sugar hydrolase and 5'-nucleotidase activities
-
?
additional information
?
-
-
5'-nucleotidase catalyzes the hydrolysis of the phosphoric ester bond of nucleoside 5'-monophosphates, such as AMP, CMP, UMP, IMP and GMP, to the corresponding nucleosides and phosphate
-
-
-
additional information
?
-
-
alcohols do not function as phosphate acceptors and suggests that the enzyme lacks transphosphorylation activity
-
?
additional information
?
-
alcohols do not function as phosphate acceptors and suggests that the enzyme lacks transphosphorylation activity
-
?
additional information
?
-
-
no dephosphorylation of araCMP and 2-fluoroadenine-9-beta-D-arabinofuranoside
-
?
additional information
?
-
no dephosphorylation of araCMP and 2-fluoroadenine-9-beta-D-arabinofuranoside
-
?
additional information
?
-
-
cN-I may play an important role in the regulation of physiological pyrimidine nucleotide pools and may also alter the therapeutic efficiacy of certain nucleoside analogs
-
?
additional information
?
-
cN-I may play an important role in the regulation of physiological pyrimidine nucleotide pools and may also alter the therapeutic efficiacy of certain nucleoside analogs
-
?
additional information
?
-
-
major role in regulation of adenosine concentrations on airway surfaces
-
?
additional information
?
-
-
patients with nucleotidase-associated pervasive developmental disorder exhibit altered electrophoretic mobility of cytosolic 5'-nucleotidase
-
?
additional information
?
-
-
the enzyme contributes to function of endothelial cells by inhibiting platelet aggregation in cooperation with ATP diphosphohydrolase, which degrades ADP to AMP
-
?
additional information
?
-
cytosolic 5'-nucleotidase II catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates
-
-
-
additional information
?
-
-
Usha, Pho5, Sdt1 and Phm8 are phosphate starvation-induced 5'-nucleotidases with diverse substrate specificities that liberate phosphate under phosphate starvation conditions
-
-
-
additional information
?
-
structural basis for the substrate specificity of cN-II: Arg202, Asp206, and Phe157 seem to be important residues for purine/pyrimidine selectivity
-
-
-
additional information
?
-
poor substrate: beta-nicotinamide mononucleotide
-
-
-
additional information
?
-
activity on AMP, XMP, CMP, UMP and -nitrophenyl phosphate is poor
-
-
-
additional information
?
-
activity on AMP, XMP, CMP, UMP and -nitrophenyl phosphate is poor
-
-
-
additional information
?
-
-
5'-nucleotidase and phosphodiesterase reside in the same molecule
-
?
additional information
?
-
-
accumulation of Arg, N-acetylarginine, homoarginine and argininic acid do not alter 5'-nucleotidase activity
-
?