3.6.1.15: nucleoside-triphosphate phosphatase
This is an abbreviated version!
For detailed information about nucleoside-triphosphate phosphatase, go to the full flat file.
Word Map on EC 3.6.1.15
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3.6.1.15
-
adp
-
ectonucleotidases
-
purinergic
-
viruses
-
unwind
-
5'-nucleotidase
-
potato
-
single-stranded
-
non-structural
-
purine
-
platelet
-
virion
-
ecto-5\'-nucleotidase
-
deaminase
-
sars-cov-2
-
coronavirus
-
vaccinia
-
nucleotidase
-
toxoplasma
-
gondii
-
apyrase
-
ecto-nucleoside
-
polyproteins
-
duplex
-
nsp2
-
ecto-atpase
-
nucleocytoplasmic
-
flaviviridae
-
tachyzoite
-
ecto-enzymes
-
polynucleotides
-
3.6.1.5
-
mutt
-
guanylyltransferase
-
ntp-binding
-
reoviridae
-
primase
-
encapsidated
-
positive-stranded
-
bluetongue
-
polyu
-
entpd1
-
phosphohydrolytic
-
replicase
-
reovirus
-
ssrna
-
adpase
-
potexvirus
-
surface-located
-
medicine
-
nucleotide-mediated
- 3.6.1.15
- adp
- ectonucleotidases
-
purinergic
- viruses
-
unwind
- 5'-nucleotidase
- potato
-
single-stranded
-
non-structural
- purine
- platelet
- virion
-
ecto-5\'-nucleotidase
- deaminase
- sars-cov-2
- coronavirus
- vaccinia
-
nucleotidase
- toxoplasma
- gondii
- apyrase
-
ecto-nucleoside
- polyproteins
- duplex
- nsp2
- ecto-atpase
-
nucleocytoplasmic
- flaviviridae
- tachyzoite
-
ecto-enzymes
- polynucleotides
-
3.6.1.5
-
mutt
-
guanylyltransferase
-
ntp-binding
- reoviridae
- primase
-
encapsidated
-
positive-stranded
- bluetongue
- polyu
- entpd1
-
phosphohydrolytic
-
replicase
- reovirus
- ssrna
- adpase
- potexvirus
-
surface-located
- medicine
-
nucleotide-mediated
Reaction
Synonyms
AAA-type nucleoside triphosphatase phosphohydrolase, ankyrin repeat-rich membrane spanning protein, cell division control protein Cdc48, DEAH-box Prp22 protein, DEAH-box splicing factor Prp22, DExH-Box NTPase, DR_0079, germ-cell-specific leucine-rich repeat protein, GP086L protein, HCR-NTPase, HrpB, HrpB NTPase, human cancer-related nucleoside triphosphatase, KAP NTPase, Kidins220, kinase D interacting substance of 220 kDa, LDBPK_100150, LdNTPDase2, LINF_150005200, LiNTPDase1, LMXM_10_0170, LMXM_15_0030, LmxNTPDase1, LmxNTPDase2, M86L protein, MC100R, Mg2+-dependent NTPase, More, Msm0858, NALP14, non-specific nucleoside triphosphatase, nonstructural protein 13, NPH I, NS3, NS3 protein, NS3FL, nsp13, NTP1, NTP3, NTPase, NTPase 1, NTPase 2, NTPase-I, NTPase-II, NTPase/helicase, NTPDase, NTPDase 1, NTPDase1, NTPDase2, nucleic acid-independent nucleoside triphosphatase, nucleoside 5-triphosphatase, nucleoside triphosphatase, nucleoside triphosphatase (NTPase)/helicase, nucleoside triphosphate diphospho-hydrolase, nucleoside triphosphate diphosphohydrolase, nucleoside triphosphate diphosphohydrolase 1, nucleoside triphosphate hydrolase, nucleoside triphosphate hydrolases I, nucleoside triphosphate hydrolases II, nucleoside triphosphate phosphohydrolase, nucleoside triphosphate phosphohydrolase I, nucleoside-5-triphosphate phosphohydrolase, nucleoside-triphosphatase 1, nucleoside-triphosphatase 2, nucleotide 5'-triphosphatase, P-loop NTPase, phosphatase, nucleoside tri-, PilB, PilT, PilU, polypeptide p41, protein NS3, PVA coat protein, PVA CP, PVx coat protein, PVX CP, Rad55B, RNA-dependent nucleoside triphosphatase, SHVp41, Sso0909, T4P motor protein, type IV pilus motor protein, YtkD
ECTree
3.6.1.15 nucleoside-triphosphate phosphataseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.6.1.15 - nucleoside-triphosphate phosphatase
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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',3'-didehydro-thymidine triphosphate + H2O
2',3'-didehydro-thymidine diphosphate + phosphate
-
-
-
-
?
3'-azido-2',3'-dideoxythymidine triphosphate + H2O
3'-azido-2',3'-dideoxythymidine diphosphate + phosphate
-
-
-
-
?
dADP + H2O
dAMP + phosphate
relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
-
-
?
dCDP + H2O
dCMP + phosphate
next most preferred substrates with a relative activity of <50% compared to CDP, activity at the site of the phosphodiester bond corroborated using 31P NMR spectroscopy
-
-
?
dGDP + H2O
dGMP + phosphate
relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
-
-
?
TDP + H2O
TMP + phosphate
relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
-
-
?
ADP + H2O
AMP + phosphate
-
0.5 mM, 25% relative activity towards ADP compared to CTP, no activity towards AMP
-
-
?
ADP + H2O
AMP + phosphate
relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
-
-
?
ATP + H2O
ADP + phosphate
relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
-
-
?
ATP + H2O
ADP + phosphate
-
HCR-NTPase contains both residues E113 and G115, and has nearly identical hydrolysis rates for ATP and GTP
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant His-tagged PilB, PilT, and PilU show ATPase activity in vitro with requirement for three invariant acidic residues in the Asp Box motif, and for two invariant His residues in the His Box motif to varying extents, overview
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant His-tagged PilB, PilT, and PilU show ATPase activity in vitro with requirement for three invariant acidic residues in the Asp Box motif, and for two invariant His residues in the His Box motif to varying extents, overview
-
-
?
ATP + H2O
ADP + phosphate
-
Rad55B has a very weak ATPase activity and the activity is not stimulated by DNA
-
-
?
CDP + H2O
CMP + phosphate
-
0.5 mM, 41% relative activity towards CDP, no activity towards CMP
-
-
?
CDP + H2O
CMP + phosphate
-
0.5 mM, 41% relative activity towards CDP compared to CTP, no activity towards CMP
-
-
?
CDP + H2O
CMP + phosphate
first nudix hydrolase observed to have a marked preference for CDP and CTP, activity at the site of the phosphodiester bond corroborated using 31P NMR spectroscopy, nucleophilic substitution at the beta-phosphorus
-
-
?
CTP + H2O
CDP + phosphate
first nudix hydrolase observed to have a marked preference for CDP and CTP, activity at the site of the phosphodiester bond corroborated using 31P NMR spectroscopy, nucleophilic substitution at the beta-phosphorus
-
-
?
dATP + H2O
dADP + phosphate
relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
-
-
?
dCTP + H2O
dCDP + phosphate
next most preferred substrates with a relative activity of <50% compared to CDP, activity at the site of the phosphodiester bond corroborated using 31P NMR spectroscopy
-
-
?
dGTP + H2O
dGDP + phosphate
relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
-
-
?
GDP + H2O
GMP + phosphate
-
0.5 mM, 19% relative activity towards GDP compared to CTP, no activity towards GMP
-
-
?
GDP + H2O
GMP + phosphate
relatively low substrate activity
-
-
?
GTP + H2O
GDP + phosphate
relatively low substrate activity
-
-
?
GTP + H2O
GDP + phosphate
-
HCR-NTPase contains both residues E113 and G115, and has nearly identical hydrolysis rates for ATP and GTP
-
-
?
IDP + H2O
IMP + phosphate
-
0.5 mM, 41% relative activity towards IDP compared to CTP, 5.3% relative activity towards IMP compared to CTP
-
-
?
IDP + H2O
IMP + phosphate
-
0.5 mM, 41% relative activity towards IDP, 5.3% relative activity towards IMP compared to CTP
-
-
?
IDP + H2O
IMP + phosphate
activity at the site of the phosphodiester bond corroborated using 31P NMR spectroscopy, low substrate activity
-
-
?
TTP + H2O
TDP + phosphate
relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
-
-
?
UDP + H2O
UMP + phosphate
-
0.5 mM, 32% relative activity compared to CTP, 8.2% relative activity towards UMP compared to CTP
-
-
?
UDP + H2O
UMP + phosphate
-
0.5 mM, 32% relative activity, 8.2% relative activity towards UMP compared to CTP
-
-
?
UDP + H2O
UMP + phosphate
relative low substrate activity
-
-
?
UTP + H2O
UDP + phosphate
relative low substrate activity
-
-
?
additional information
?
-
-
substrate binding structures in presence of Mg2+, NMR structures, overview
-
-
-
additional information
?
-
-
the viral NS3 protein, i.e. NS3FL, and its N-terminal truncated version ntNS3, recombinantly expressed in Escherichia coli, contain specific polynucleotide-stimulated NTPase acitivity, the enzyme activity is essential for viral replication
-
-
?
additional information
?
-
-
the conserved motif I, GXGK232T, is required for NTPase activity of the viral NS3 protein, while motif III is not
-
-
?
additional information
?
-
-
the viral NS3 protein, i.e. NS3FL, and its N-terminal truncated version ntNS3, recombinantly expressed in Escherichia coli, contain specific polynucleotide-stimulated NTPase acitivity, the enzyme activity is essential for viral replication
-
-
?
additional information
?
-
-
the conserved motif I, GXGK232T, is required for NTPase activity of the viral NS3 protein, while motif III is not
-
-
?
additional information
?
-
-
the enzyme is involved in RNA replication and capping, overview
-
-
?
additional information
?
-
-
multifunctional enzyme showing nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase activities
-
-
?
additional information
?
-
-
the multifunctional enzyme shows RNA helicase, nucleotide 5'-triphosphatase, and RNA 5'-triphosphatase activities, which are located on the C-terminal 54-kDa domain, overview
-
-
?
additional information
?
-
HrpB contains a unique C-terminal region, exhibits a preference for hydrolyzing pyrimidic over puric NTPs, and binds single-stranded RNA but does not unwind various model RNAs in vitro. HrpB binds RNA but not DNA. NTPase activity and NTP substrate specificity of HrpB, overview. HrpB may be a weak RNA helicase that is unable to unwind the extended duplex regions in RNA30ovh19 or U4/U6 di-snRNA, is unable to overcome additional stem loops in U4/U6 di-snRNA overhangs, may require longer single-stranded regions to efficiently engage a substrate, or may indeed unwind RNAs in 5'-to-3' direction. In the presence of ssRNA, the enzyme is able to hydrolyze ATP, GTP, UTP, and CTP. Interestingly, the NTPase activity is higher for pyrimidic than for puric NTPs
-
-
-
additional information
?
-
-
HrpB contains a unique C-terminal region, exhibits a preference for hydrolyzing pyrimidic over puric NTPs, and binds single-stranded RNA but does not unwind various model RNAs in vitro. HrpB binds RNA but not DNA. NTPase activity and NTP substrate specificity of HrpB, overview. HrpB may be a weak RNA helicase that is unable to unwind the extended duplex regions in RNA30ovh19 or U4/U6 di-snRNA, is unable to overcome additional stem loops in U4/U6 di-snRNA overhangs, may require longer single-stranded regions to efficiently engage a substrate, or may indeed unwind RNAs in 5'-to-3' direction. In the presence of ssRNA, the enzyme is able to hydrolyze ATP, GTP, UTP, and CTP. Interestingly, the NTPase activity is higher for pyrimidic than for puric NTPs
-
-
-
additional information
?
-
-
substrate binding structures in presence of Mg2+, NMR structures, overview
-
-
-
additional information
?
-
-
multifunctional protein, possessing protease, NTPase and helicase activities. These activities are essential for the virus life cycle
-
-
?
additional information
?
-
-
multifunctional protein, possessing protease, NTPase and helicase activities. Different stereoselectivity in nucleoside triphosphate utilisation suggests that NTPase and helicase activities are coupled by a nucleotide-dependent rate limiting step
-
-
?
additional information
?
-
-
multifunctional enzyme showing nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase activities
-
-
?
additional information
?
-
-
HCR-NTPase is a non-selective NTPase with only slightly higher activity for purine nucleoside triphosphates, and with a comparatively low rate of hydrolysis, structural basis of HCR-NTPase activity, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes all natural ribonucleotides and nucleotides, the enzyme also mediates RNA 5'-triphosphatase activity using the NTPase active site, this activity is inhibited by ATP, overview
-
-
?
additional information
?
-
-
multifunctional enzyme showing nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase activities
-
-
?
additional information
?
-
-
the virus core particles, an icosahedral multienzyme complex, and the transcriptase cofactor my2 show nucleoside triphosphatase activity
-
-
?
additional information
?
-
-
the virus core particles, an icosahedral multienzyme complex, and the transcriptase cofactor my2 show nucleoside triphosphatase activity
-
-
?
additional information
?
-
-
ATP and GTP are preferred over CTP and UTP for hydrolysis by MNV NS3, with ATP being the most favoured substrate. The MNV NS3 has an NTPase-independent RNA chaperone-like activity. NS3 destabilizes double-stranded RNA in the presence of Mg2+ or Mn2+ in an NTP-independent manner
-
-
-
additional information
?
-
enzyme Msm0858 is a magnesium-dependent ATPase and is active with all nucleoside triphosphates (NTPs) and deoxynucleoside triphosphates (dNTPs) as substrates
-
-
-
additional information
?
-
-
enzyme Msm0858 is a magnesium-dependent ATPase and is active with all nucleoside triphosphates (NTPs) and deoxynucleoside triphosphates (dNTPs) as substrates
-
-
-
additional information
?
-
enzyme Msm0858 is a magnesium-dependent ATPase and is active with all nucleoside triphosphates (NTPs) and deoxynucleoside triphosphates (dNTPs) as substrates
-
-
-
additional information
?
-
enzyme Msm0858 is a magnesium-dependent ATPase and is active with all nucleoside triphosphates (NTPs) and deoxynucleoside triphosphates (dNTPs) as substrates
-
-
-
additional information
?
-
-
the coat protein of the plant virus exhibits NTPase activity, the coat proteins are involved in different stages of the viral life cycle such as virion assembyl, replication, movement, vector transmission, and regulation of host defense response
-
-
?
additional information
?
-
-
the coat protein of the plant virus exhibits NTPase activity, the coat proteins are involved in different stages of the viral life cycle such as virion assembyl, replication, movement, vector transmission, and regulation of host defense response
-
-
?
additional information
?
-
-
the enzyme hydrolyzes ribonucleotides and deoxyribonucleotides
-
-
?
additional information
?
-
Sso0909 is an orthologue of the eukaryotic endosomal sorting complex required for transport, ESCRT, ATPase Vps4, i.e. vacular protein sorting 4. Sso0909 is not involved in a cellular protection mechanism, but is required during normal cell growth
-
-
?
additional information
?
-
-
Sso0909 is an orthologue of the eukaryotic endosomal sorting complex required for transport, ESCRT, ATPase Vps4, i.e. vacular protein sorting 4. Sso0909 is not involved in a cellular protection mechanism, but is required during normal cell growth
-
-
?
additional information
?
-
-
the N-terminal AAA+ ATPase domains of Orc1/Cdc6 proteins show DNA-binding activities and functional interactions with other Cdc6 proteins, on duplex DNA substrates derived from the origins of Sulfolobus solfataricus, overview. ATPase domain of Cdc6-2 retains both DNA-binding activity and regulating effect on that of Cdc6-3 at the origin, overview
-
-
?
additional information
?
-
-
Cdc6-1 significantly improves DNA-binding activity at the forked substrate, but only shows a very weak ability towards the blunt DNA substrate
-
-
?
additional information
?
-
-
the DEAH-box splicing factor Prp22 is important in the second transesterification step of pre-mRNA splicing and is essential for release of mature mRNA from the splicosome
-
-
?
additional information
?
-
-
DEAH-box splicing factor Prp22 shows NTPase, RNA-binding, and RNA helicase activities, ATP binding leads to dissociation of the protein from RNA, RNA binding activates the NTPase activity
-
-
?
additional information
?
-
the enzyme does not possess helicase activity
-
-
?
additional information
?
-
-
the enzyme does not possess helicase activity
-
-
?
additional information
?
-
-
Rad55B also performs DNA repair, DNA binding using single-stranded or double-stranded 84mer oligonucleotide as substrate, Rad55B is a homologue of RadA, that is able to perform DNA strand exchanges using circular single-stranded M13mp18 virion DNA as substrate, overview
-
-
?
additional information
?
-
the enzymatic effect of NTPases is independent of the species or cell type background of the reporter assay, as reflected by very similar results in both murine RAW264.7 macrophages and human HeLa cells
-
-
-
additional information
?
-
the enzymatic effect of NTPases is independent of the species or cell type background of the reporter assay, as reflected by very similar results in both murine RAW264.7 macrophages and human HeLa cells
-
-
-
additional information
?
-
-
the enzymatic effect of NTPases is independent of the species or cell type background of the reporter assay, as reflected by very similar results in both murine RAW264.7 macrophages and human HeLa cells
-
-
-
additional information
?
-
nucleoside phosphorylase activity was monitored spectrophotometrically by following orthophosphate release using the malachite green method
-
-
-
additional information
?
-
-
nucleoside phosphorylase activity was monitored spectrophotometrically by following orthophosphate release using the malachite green method
-
-
-
additional information
?
-
nucleoside triphosphate phosphohydrolase I (NPH I) is an essential component of the early gene transcription complex. NPH I hydrolyzes ATP to release transcripts during transcription termination. The ATPase activity of NPH I requires single-stranded (ss) DNA as a cofactor. Isolated NPHI also acts as a 5' to 3' translocase on single-stranded DNA. In vitro transcription on templates that lack portions of the nontemplate strand within the transcription bubble shows that the upstream portion of the transcription bubble is required for efficient NPH I-mediated transcript release. Complementarity between the template and non-template strands in this region is also required for NPHI-mediated transcript release. dsDNA Ter29 is the in vitro transcription template, Ter29 contains a strong early promoter joined to a 20-base G-less cassette followed by 4 G residues from positions +21 to +24. The G-less cassette is followed by a 57-base A-less cassette, construction of oligonucleotide-based transcription templates, overview. Residues of the non-template DNA within the upstream region of the transcription bubble are required for NPH I to efficiently (over 50%) release nascent RNA from the vaccinia early gene ternary complex. The requirement for the non-template strand in the transcription bubble for transcript release is not NPH I-specific. The ability of NPH I to disrupt the streptavidin-biotin interaction is also tested on the single-stranded DNAs that are biotinylated at either the 5' or 3' end. Ribonucleotides within the non-template strand of transcription bubble specifically inhibits NPH I-mediated transcript release. Transcript release requires complementarity between the T and NT strands within the upstream region of the transcription bubble
-
-
-
additional information
?
-
-
nucleoside triphosphate phosphohydrolase I (NPH I) is an essential component of the early gene transcription complex. NPH I hydrolyzes ATP to release transcripts during transcription termination. The ATPase activity of NPH I requires single-stranded (ss) DNA as a cofactor. Isolated NPHI also acts as a 5' to 3' translocase on single-stranded DNA. In vitro transcription on templates that lack portions of the nontemplate strand within the transcription bubble shows that the upstream portion of the transcription bubble is required for efficient NPH I-mediated transcript release. Complementarity between the template and non-template strands in this region is also required for NPHI-mediated transcript release. dsDNA Ter29 is the in vitro transcription template, Ter29 contains a strong early promoter joined to a 20-base G-less cassette followed by 4 G residues from positions +21 to +24. The G-less cassette is followed by a 57-base A-less cassette, construction of oligonucleotide-based transcription templates, overview. Residues of the non-template DNA within the upstream region of the transcription bubble are required for NPH I to efficiently (over 50%) release nascent RNA from the vaccinia early gene ternary complex. The requirement for the non-template strand in the transcription bubble for transcript release is not NPH I-specific. The ability of NPH I to disrupt the streptavidin-biotin interaction is also tested on the single-stranded DNAs that are biotinylated at either the 5' or 3' end. Ribonucleotides within the non-template strand of transcription bubble specifically inhibits NPH I-mediated transcript release. Transcript release requires complementarity between the T and NT strands within the upstream region of the transcription bubble
-
-
-
additional information
?
-
nucleoside triphosphate phosphohydrolase I (NPH I) is an essential component of the early gene transcription complex. NPH I hydrolyzes ATP to release transcripts during transcription termination. The ATPase activity of NPH I requires single-stranded (ss) DNA as a cofactor. Isolated NPHI also acts as a 5' to 3' translocase on single-stranded DNA. In vitro transcription on templates that lack portions of the nontemplate strand within the transcription bubble shows that the upstream portion of the transcription bubble is required for efficient NPH I-mediated transcript release. Complementarity between the template and non-template strands in this region is also required for NPHI-mediated transcript release. dsDNA Ter29 is the in vitro transcription template, Ter29 contains a strong early promoter joined to a 20-base G-less cassette followed by 4 G residues from positions +21 to +24. The G-less cassette is followed by a 57-base A-less cassette, construction of oligonucleotide-based transcription templates, overview. Residues of the non-template DNA within the upstream region of the transcription bubble are required for NPH I to efficiently (over 50%) release nascent RNA from the vaccinia early gene ternary complex. The requirement for the non-template strand in the transcription bubble for transcript release is not NPH I-specific. The ability of NPH I to disrupt the streptavidin-biotin interaction is also tested on the single-stranded DNAs that are biotinylated at either the 5' or 3' end. Ribonucleotides within the non-template strand of transcription bubble specifically inhibits NPH I-mediated transcript release. Transcript release requires complementarity between the T and NT strands within the upstream region of the transcription bubble
-
-
-
additional information
?
-
-
helicase activity, the enzyme catalyzes the unwinding of DNA duplex
-
-
?
additional information
?
-
-
multifunctional enzyme showing nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase activities
-
-
?
