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Information on EC 3.1.3.5 - 5'-nucleotidase and Organism(s) Bos taurus
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3.1.3.5 5'-nucleotidaseIUBMB Comments
Wide specificity for 5'-nucleotides.
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Word Map
- 3.1.3.5
- nucleoside
- adp
- deaminase
- triphosphate
-
purinergic
-
ecto-5\'-nucleotidase
- lymphocyte
- endothelial
- phosphodiesterase
- ntpdases
- agonist
-
diphosphohydrolase
- erythrocyte
- adenylate
- inosine
- platelet
- phosphorylase
- na+
-
cytochemical
- glucose-6-phosphatase
- 5'-monophosphate
- hypoxanthine
-
histochemistry
-
concanavalin
- acetylcholinesterase
- apyrase
-
ecto-enzymes
-
synaptosomes
- 5'-diphosphate
- adpase
- ecto-atpase
- suramin
- mg2+-atpase
- deoxycytidine
-
k+-atpase
- dpcpx
- dipyridamole
-
ouabain-sensitive
-
purinoceptors
- phosphomonoesterase
- sarcolemma
-
plasma-membrane
-
neuromodulator
- antivenoms
-
ppads
- ehna
- 8-cyclopentyl-1,3-dipropylxanthine
-
ectonucleotide
-
8-phenyltheophylline
- nutrition
- hgprt
- medicine
- pharmacology
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
5'-nucleotidase, ecto-5'-nucleotidase, ectonucleotidase, 5'nucleotidase, 5'-nt, cn-ii, ecto-nucleotidase, pyrimidine 5'-nucleotidase, cytosolic 5'-nucleotidase, ampase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-adenylic phosphatase
-
-
-
-
5'-AMP nucleotidase
-
-
-
-
5'-AMPase
-
-
-
-
5'-mononucleotidase
-
-
-
-
5'nucleotidase
-
-
-
-
adenosine 5'-monophosphatase
-
-
-
-
adenosine 5'-phosphatase
-
-
-
-
adenosine monophosphatase
-
-
-
-
AMP phosphatase
-
-
-
-
AMP phosphohydrolase
-
-
-
-
AMPase
-
-
-
-
CD73 antigen
-
-
-
-
cN-II
ecto-5'-nucleotidase
IMP 5'-nucleotidase
-
-
-
-
snake venom 5'-nucleotidase
-
-
-
-
thymidine monophosphate nucleotidase
-
-
-
-
UMPase
-
-
-
-
uridine 5'-nucleotidase
-
-
-
-
ecto-5'-nucleotidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
5'-ribonucleotide phosphohydrolase
Wide specificity for 5'-nucleotides.
CAS REGISTRY NUMBER
COMMENTARY
9027-73-0
-
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
5'-IMP + H2O
inosine + phosphate
-
preferred substrate of cytosolic thymus enzyme
-
-
?
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
-
?
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
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
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe2+
-
oxidative inactivation in a Fe2+/GSH system may be related to the selective association of Fe2+ and thiols to the enzyme molecule
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha,beta-methylene-adenosine 5'-diphosphate
-
inhibits isoforms: 5'-NT-1, 5'-NT-2, 5'-NT-3, 5'-NT-4
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
5'-IMP
pH not specified in the publication, temperature not specified in the publication, recombinant mutant K311A
0.05
5'-IMP
pH not specified in the publication, temperature not specified in the publication, recombinant mutant G319D
0.06
5'-IMP
pH not specified in the publication, temperature not specified in the publication, recombinant mutant Y115A
0.1
5'-IMP
pH not specified in the publication, temperature not specified in the publication, recombinant wild-type enzyme and mutant D396A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 5NTD_BOVIN
574
1
62966
Swiss-Prot
Secretory Pathway (Reliability: 3)
5NTC_BOVIN
560
0
64841
Swiss-Prot
other Location (Reliability: 2)
Q32L46_BOVIN
297
0
33967
TrEMBL
other Location (Reliability: 2)
A0A3Q1MUV7_BOVIN
362
1
41234
TrEMBL
other Location (Reliability: 2)
F1MLB9_BOVIN
300
0
34752
TrEMBL
other Location (Reliability: 3)
A0A3Q1MCG3_BOVIN
574
1
63050
TrEMBL
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
-
liver plasma membrane, SDS-PAGE after cross-linking with dimethylsuberimidate
68000
-
2 * 68000, the subunits in eNT dimers are not linked by disulfide bridges, but by non-covalent bonds. Dissociation precedes inactivation and unfolding, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
the active tetramer is formed by interaction between two identical dimers via interface B: this interface contains 28 aminoacid residues, of which 8 make hydrogen bonds
dimer
-
2 * 68000, the subunits in eNT dimers are not linked by disulfide bridges, but by non-covalent bonds. Dissociation precedes inactivation and unfolding, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
differential glycosylation, especially in the oligosaccharides linked to Asn403, an increase in sialylated glycans, together with a decrease in high-mannose structures is observed arising from 5'-NT-1 to 5'-NT-4
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D351E
-
strong decrease in nucleotidase activity, strong reduction in affinity towards Mg2+
D356E
-
strong decrease in nucleotidase activity, strong reduction in affinity towards Mg2+
D396A
site-directed mutagenesis, the mutant is only activable by 2,3-bisphosphoglycerate
G319D
site-directed mutagenesis, the mutant shows altered kinetics compare to the wild-type enzyme
K311A
site-directed mutagenesis, the mutant shows altered kinetics compare to the wild-type enzyme
M53I
-
lowest nucleotidase vs. phosphotransferase activity ratio of all mutants tested
N154D
site-directed mutagenesis, the mutant shows a decrease in the value of K50 for Mg2+ compared to the wild-type enzyme
Y115A
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
membrane-bound enzyme is less thermostable than solubilized
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inhibition by CuCl2, 5,5-dithiobis-(2-nitro-benzoic acid) is reverted by presence of reducing agent
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
target for a number of therapeutic drugs since increased levels of the enzyme correlate with various disease states
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zekri, M.; Harb, J.; Bernard, S.; Meflah, K.
Purification of bovine liver cytosolic 5'-nucleotidase. Kinetic and structural studies as compared to the membrane isoenzyme
Eur. J. Biochem.
172
93-99
1988
Bos taurus
Harb, J.; Meflah, K.; Duflos, Y.; Bernard, S.
Purification and properties of bovine liver plasma membrane 5' nucleotidase
Eur. J. Biochem.
137
131-138
1983
Bos taurus
Fini, C.; Coli, M.; Floridi, A.; DAuria, S.; Staiano, M.; Nucci, R.; Rossi, M.
Temperature effects on the structural and functional properties of GPI-anchored and anchor-less bull seminal plasma ecto-5'-nucleotidase
J. Biochem.
123
269-274
1998
Bos taurus
Pesi, R.; Baiocchi, C.; Allegrini, S.; Moretti, E.; Sgarrella, F.; Camici, M.; Tozzi, M.G.
Identification, separation and characterization of two forms of cytosolic 5'-nucleotidase/nucleoside phosphotransferase in calf thymus
Biol. Chem.
379
699-704
1998
Bos taurus
Fini, C.; Talamo, F.; Cherri, S.; Coli, M.; Floridi, A.; Ferrara, L.; Scaloni, A.
Biochemical and mass spectrometric characterization of soluble ecto-5'-nucleotidase from bull seminal plasma
Biochem. J.
372
443-451
2003
Bos taurus
Martinez-Martinez, A.; Munoz-Delgado, E.; Campoy, F.J.; Flores-Flores, C.; Rodriguez-Lopez, J.N.; Fini, C.; Vidal, C.J.
The ecto-5'-nucleotidase subunits in dimers are not linked by disulfide bridges but by non-covalent bonds
Biochim. Biophys. Acta
1478
300-308
2000
Bos taurus
Allegrini, S.; Scaloni, A.; Ferrara, L.; Pesi, R.; Pinna, P.; Sgarrella, F.; Camici, M.; Eriksson, S.; Tozzi, M.G.
Bovine cytosolic 5'-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate
J. Biol. Chem.
276
33526-33532
2001
Bos taurus
Liu, X.W.; Sok, D.E.
Oxidative inactivation of brain ecto-5'-nucleotidase by thiols/Fe2+ system
Neurochem. Res.
25
1475-1484
2000
Bos taurus
Allegrini, S.; Scaloni, A.; Careddu, M.G.; Cuccu, G.; D'Ambrosio, C.; Pesi, R.; Camici, M.; Ferrara, L.; Tozzi, M.G.
Mechanistic studies on bovine cytosolic 5'-nucleotidase II, an enzyme belonging to the HAD superfamily
Eur. J. Biochem.
271
4881-4891
2004
Bos taurus
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