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Information on EC 3.6.1.15 - nucleoside-triphosphate phosphatase
for references in articles please use BRENDA:EC3.6.1.15
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.15 nucleoside-triphosphate phosphatase
IUBMB Comments
The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. Also hydrolyses nucleoside diphosphates, thiamine diphosphate and FAD. The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin .
The enzyme appears in viruses and cellular organisms
- 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
showSynonyms
ntpase, ntpdase, nucleoside triphosphatase, ntpdase1, ntpdase2, nsp13, kidins220, nucleoside triphosphate diphosphohydrolase, nucleoside triphosphate hydrolase, pvx cp, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAA-type nucleoside triphosphatase phosphohydrolase
ankyrin repeat-rich membrane spanning protein
cell division control protein Cdc48
GP086L protein
-
-
-
-
KAP NTPase
Kidins220
kinase D interacting substance of 220 kDa
LDBPK_100150
LdNTPDase2
LMXM_10_0170
LMXM_15_0030
LmxNTPDase1
LmxNTPDase2
M86L protein
-
-
-
-
MC100R
-
-
-
-
Msm0858
NPH I
NS3
NS3 protein
NS3FL
Ntdp
NTPase
NTPase-I
NTPase/helicase
NTPDase
NTPDase 1
NTPDase1
NTPDase2
nucleoside 5-triphosphatase
-
-
-
-
nucleoside triphosphatase
nucleoside triphosphate diphosphohydrolase
nucleoside triphosphate diphosphohydrolase 1
nucleoside triphosphate hydrolase
nucleoside triphosphate phosphohydrolase
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-
-
-
nucleoside triphosphate phosphohydrolase I
nucleoside-5-triphosphate phosphohydrolase
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-
-
-
P-loop NTPase
phosphatase, nucleoside tri-
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-
-
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PilB
PilT
PilU
SA1684
Sc4828
T4P motor protein
type IV pilus motor protein
YtkD
additional information
AAA-type nucleoside triphosphatase phosphohydrolase
-
-
NTPase
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-
-
-
additional information
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the enzyme belongs to the KAP family of NTPases
additional information
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the enzyme is a member of the Nudix hydrolase superfamily
additional information
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the enzyme is a member of the Nudix hydrolase superfamily
-
additional information
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the enzyme belongs to the KAP family of NTPases
additional information
-
the enzyme is a nonstructural protein 3, NS3 of family Flaviviridae members
additional information
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the enzyme is a nonstructural protein 3, NS3 of family Flaviviridae members
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additional information
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the enzyme belongs to the KAP family of NTPases
additional information
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the enzyme belongs to the KAP family of NTPases
additional information
-
the enzyme belongs to the KAP family of NTPases
additional information
-
the enzyme belongs to the KAP family of NTPases
additional information
-
the enzyme belongs to the KAP family of NTPases
additional information
-
the enzyme belongs to the KAP family of NTPases
additional information
-
the enzyme belongs to the KAP family of NTPases
additional information
-
the enzyme belongs to the KAP family of NTPases
additional information
-
the enzyme belongs to the KAP family of NTPases
additional information
-
the protein is a member of the LRR-replete NACHT nucleoside triphosphatase family
additional information
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PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily
additional information
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the enzyme belongs to the KAP family of NTPases
additional information
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the enzyme belongs to the KAP family of NTPases
additional information
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the enzyme belongs to the KAP family of NTPases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a nucleoside triphosphate + H2O = a nucleoside diphosphate + phosphate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
pyrimidine deoxyribonucleotides biosynthesis from CTP, pyrimidine deoxyribonucleotides de novo biosynthesis I, pyrimidine deoxyribonucleotides de novo biosynthesis III, pyrimidine deoxyribonucleotides de novo biosynthesis IV, UTP and CTP dephosphorylation I
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SYSTEMATIC NAME
IUBMB Comments
unspecific diphosphate phosphohydrolase
The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. Also hydrolyses nucleoside diphosphates, thiamine diphosphate and FAD. The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin [5].
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CAS REGISTRY NUMBER
COMMENTARY
9075-51-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: -
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?
3'-azido-2',3'-dideoxythymidine triphosphate + H2O
3'-azido-2',3'-dideoxythymidine diphosphate + phosphate
-
Substrates: -
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?
dADP + H2O
dAMP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
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?
dCDP + H2O
dCMP + phosphate
Substrates: 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
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?
dGDP + H2O
dGMP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
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?
ssDNA + H2O
?
-
Substrates: removal of gamma-phosphate from nucleotides
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?
ssRNA + H2O
?
-
Substrates: removal of gamma-phosphate from nucleotides
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?
TDP + H2O
TMP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
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?
XTP + H2O
XDP + phosphate
-
Substrates: 0.5 mM, 40% relative activity compared to CTP
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?
ADP + H2O
AMP + phosphate
-
Substrates: 0.5 mM, 25% relative activity towards ADP compared to CTP, no activity towards AMP
Products: -
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?
ADP + H2O
AMP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
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?
ADP + H2O
AMP + phosphate
Substrates: -
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ir
ATP + H2O
ADP + phosphate
-
Substrates: 0.5 mM, 32% relative activity compared to CTP
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?
ATP + H2O
ADP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
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?
ATP + H2O
ADP + phosphate
-
Substrates: HCR-NTPase contains both residues E113 and G115, and has nearly identical hydrolysis rates for ATP and GTP
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?
ATP + H2O
ADP + phosphate
-
Substrates: NTPase activity
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?
ATP + H2O
ADP + phosphate
Substrates: -
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ir
ATP + H2O
ADP + phosphate
Substrates: -
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?
ATP + H2O
ADP + phosphate
Substrates: -
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?
ATP + H2O
ADP + phosphate
Orthopoxvirus vaccinia Western Reserve
Substrates: -
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?
ATP + H2O
ADP + phosphate
-
Substrates: ATP in form of MgATP2-
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?
ATP + H2O
ADP + phosphate
-
Substrates: 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
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?
ATP + H2O
ADP + phosphate
-
Substrates: 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
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?
ATP + H2O
ADP + phosphate
Substrates: -
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?
ATP + H2O
ADP + phosphate
-
Substrates: Rad55B has a very weak ATPase activity and the activity is not stimulated by DNA
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?
CDP + H2O
CMP + phosphate
-
Substrates: 0.5 mM, 41% relative activity towards CDP, no activity towards CMP
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?
CDP + H2O
CMP + phosphate
-
Substrates: 0.5 mM, 41% relative activity towards CDP compared to CTP, no activity towards CMP
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?
CDP + H2O
CMP + phosphate
Substrates: 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
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?
CTP + H2O
CDP + phosphate
-
Substrates: 0.5 mM, 100% relative activity
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?
CTP + H2O
CDP + phosphate
Substrates: 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
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?
CTP + H2O
CDP + phosphate
Substrates: -
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?
CTP + H2O
CDP + phosphate
Substrates: -
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?
CTP + H2O
CDP + phosphate
Substrates: about 35% of activity with ATP
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?
dATP + H2O
dADP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
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?
dATP + H2O
dADP + phosphate
Substrates: -
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?
dATP + H2O
dADP + phosphate
Substrates: -
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?
dCTP + H2O
dCDP + phosphate
Substrates: 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
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?
dGTP + H2O
dGDP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
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?
dGTP + H2O
dGDP + phosphate
Substrates: best substrate
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?
GDP + H2O
GMP + phosphate
-
Substrates: 0.5 mM, 19% relative activity towards GDP compared to CTP, no activity towards GMP
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?
GDP + H2O
GMP + phosphate
Substrates: relatively low substrate activity
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?
GTP + H2O
GDP + phosphate
-
Substrates: 0.5 mM, 30% relative activity compared to CTP
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?
GTP + H2O
GDP + phosphate
Substrates: relatively low substrate activity
Products: -
Products: -
?
GTP + H2O
GDP + phosphate
-
Substrates: HCR-NTPase contains both residues E113 and G115, and has nearly identical hydrolysis rates for ATP and GTP
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?
GTP + H2O
GDP + phosphate
Substrates: -
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?
GTP + H2O
GDP + phosphate
Substrates: -
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?
GTP + H2O
GDP + phosphate
Substrates: about 90% of activity with ATP
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?
IDP + H2O
IMP + phosphate
-
Substrates: 0.5 mM, 41% relative activity towards IDP compared to CTP, 5.3% relative activity towards IMP compared to CTP
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?
IDP + H2O
IMP + phosphate
-
Substrates: 0.5 mM, 41% relative activity towards IDP, 5.3% relative activity towards IMP compared to CTP
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?
IDP + H2O
IMP + phosphate
Substrates: activity at the site of the phosphodiester bond corroborated using 31P NMR spectroscopy, low substrate activity
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?
ITP + H2O
IDP + phosphate
-
Substrates: 0.5 mM, 58% relative activity compared to CTP
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?
RNA + H2O
?
-
Substrates: removal of the gamma-phosphate
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?
RNA + H2O
?
-
Substrates: removal of the gamma-phosphate
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?
TTP + H2O
TDP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
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?
UDP + H2O
UMP + phosphate
-
Substrates: 0.5 mM, 32% relative activity compared to CTP, 8.2% relative activity towards UMP compared to CTP
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?
UDP + H2O
UMP + phosphate
-
Substrates: 0.5 mM, 32% relative activity, 8.2% relative activity towards UMP compared to CTP
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?
UDP + H2O
UMP + phosphate
Substrates: relative low substrate activity
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?
UTP + H2O
UDP + phosphate
-
Substrates: 0.5 mM, 66% relative activity compared to CTP
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?
UTP + H2O
UDP + phosphate
Substrates: relative low substrate activity
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?
UTP + H2O
UDP + phosphate
Substrates: -
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?
UTP + H2O
UDP + phosphate
Substrates: -
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?
UTP + H2O
UDP + phosphate
Substrates: about 35% of activity with ATP
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?
additional information
?
-
-
Substrates: substrate binding structures in presence of Mg2+, NMR structures, overview
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?
additional information
?
-
-
Substrates: 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
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?
additional information
?
-
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Substrates: the conserved motif I, GXGK232T, is required for NTPase activity of the viral NS3 protein, while motif III is not
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?
additional information
?
-
-
Substrates: the enzyme is involved in RNA replication and capping, overview
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?
additional information
?
-
-
Substrates: multifunctional enzyme showing nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase activities
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?
additional information
?
-
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Substrates: 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
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?
additional information
?
-
-
Substrates: substrate binding structures in presence of Mg2+, NMR structures, overview
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?
additional information
?
-
Substrates: 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
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additional information
?
-
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Substrates: 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
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?
additional information
?
-
-
Substrates: multifunctional protein, possessing protease, NTPase and helicase activities. These activities are essential for the virus life cycle
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?
additional information
?
-
-
Substrates: 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
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?
additional information
?
-
-
Substrates: multifunctional enzyme showing nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase activities
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?
additional information
?
-
-
Substrates: 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
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additional information
?
-
-
Substrates: 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
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?
additional information
?
-
-
Substrates: multifunctional enzyme showing nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase activities
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?
additional information
?
-
-
Substrates: the virus core particles, an icosahedral multienzyme complex, and the transcriptase cofactor my2 show nucleoside triphosphatase activity
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additional information
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-
-
Substrates: 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
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?
additional information
?
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Substrates: enzyme Msm0858 is a magnesium-dependent ATPase and is active with all nucleoside triphosphates (NTPs) and deoxynucleoside triphosphates (dNTPs) as substrates
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additional information
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Substrates: enzyme Msm0858 is a magnesium-dependent ATPase and is active with all nucleoside triphosphates (NTPs) and deoxynucleoside triphosphates (dNTPs) as substrates
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additional information
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Substrates: 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
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additional information
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Orthopoxvirus vaccinia Western Reserve
Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: the enzyme hydrolyzes ribonucleotides and deoxyribonucleotides
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: Cdc6-1 significantly improves DNA-binding activity at the forked substrate, but only shows a very weak ability towards the blunt DNA substrate
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additional information
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Substrates: 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
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additional information
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-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not possess helicase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not possess helicase activity
Products: -
Products: -
?
additional information
?
-
Substrates: Sc4828 shows hydrolysis activity to ADP, ATP, and GDP but not GTP. The closed substrate-binding pocket of Sc4828 cannot accommodate a nucleoside triphosphate with guanosine
Products: -
Products: -
-
additional information
?
-
Substrates: Sc4828 shows hydrolysis activity to ADP, ATP, and GDP but not GTP. The closed substrate-binding pocket of Sc4828 cannot accommodate a nucleoside triphosphate with guanosine
Products: -
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: nucleoside phosphorylase activity was monitored spectrophotometrically by following orthophosphate release using the malachite green method
Products: -
Products: -
?
additional information
?
-
-
Substrates: nucleoside phosphorylase activity was monitored spectrophotometrically by following orthophosphate release using the malachite green method
Products: -
Products: -
?
additional information
?
-
-
Substrates: helicase activity, the enzyme catalyzes the unwinding of DNA duplex
Products: -
Products: -
?
additional information
?
-
-
Substrates: helicase activity with RNA duplex
Products: -
Products: -
?
additional information
?
-
-
Substrates: multifunctional enzyme showing nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase activities
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dADP + H2O
dAMP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
Products: -
?
dCDP + H2O
dCMP + phosphate
Substrates: 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
Products: -
Products: -
?
dGDP + H2O
dGMP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
Products: -
?
TDP + H2O
TMP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
Products: -
?
XTP + H2O
XDP + phosphate
-
Substrates: 0.5 mM, 40% relative activity compared to CTP
Products: -
Products: -
?
ADP + H2O
AMP + phosphate
-
Substrates: 0.5 mM, 25% relative activity towards ADP compared to CTP, no activity towards AMP
Products: -
Products: -
?
ADP + H2O
AMP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
Products: -
?
ADP + H2O
AMP + phosphate
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
-
Substrates: 0.5 mM, 32% relative activity compared to CTP
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: NTPase activity
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Orthopoxvirus vaccinia Western Reserve
Substrates: -
Products: -
Products: -
?
CDP + H2O
CMP + phosphate
-
Substrates: 0.5 mM, 41% relative activity towards CDP, no activity towards CMP
Products: -
Products: -
?
CDP + H2O
CMP + phosphate
Substrates: 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
Products: -
Products: -
?
CTP + H2O
CDP + phosphate
-
Substrates: 0.5 mM, 100% relative activity
Products: -
Products: -
?
CTP + H2O
CDP + phosphate
Substrates: 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
Products: -
Products: -
?
CTP + H2O
CDP + phosphate
Substrates: -
Products: -
Products: -
?
CTP + H2O
CDP + phosphate
Substrates: -
Products: -
Products: -
?
dATP + H2O
dADP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
Products: -
?
dATP + H2O
dADP + phosphate
Substrates: -
Products: -
Products: -
?
dATP + H2O
dADP + phosphate
Substrates: -
Products: -
Products: -
?
dCTP + H2O
dCDP + phosphate
Substrates: 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
Products: -
Products: -
?
dGTP + H2O
dGDP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
Products: -
?
dGTP + H2O
dGDP + phosphate
Substrates: best substrate
Products: -
Products: -
?
GDP + H2O
GMP + phosphate
-
Substrates: 0.5 mM, 19% relative activity towards GDP compared to CTP, no activity towards GMP
Products: -
Products: -
?
GDP + H2O
GMP + phosphate
Substrates: relatively low substrate activity
Products: -
Products: -
?
GTP + H2O
GDP + phosphate
-
Substrates: 0.5 mM, 30% relative activity compared to CTP
Products: -
Products: -
?
GTP + H2O
GDP + phosphate
Substrates: relatively low substrate activity
Products: -
Products: -
?
GTP + H2O
GDP + phosphate
Substrates: -
Products: -
Products: -
?
GTP + H2O
GDP + phosphate
Substrates: -
Products: -
Products: -
?
IDP + H2O
IMP + phosphate
-
Substrates: 0.5 mM, 41% relative activity towards IDP compared to CTP, 5.3% relative activity towards IMP compared to CTP
Products: -
Products: -
?
IDP + H2O
IMP + phosphate
Substrates: activity at the site of the phosphodiester bond corroborated using 31P NMR spectroscopy, low substrate activity
Products: -
Products: -
?
ITP + H2O
IDP + phosphate
-
Substrates: 0.5 mM, 58% relative activity compared to CTP
Products: -
Products: -
?
RNA + H2O
?
-
Substrates: removal of the gamma-phosphate
Products: -
Products: -
?
RNA + H2O
?
-
Substrates: removal of the gamma-phosphate
Products: -
Products: -
?
TTP + H2O
TDP + phosphate
Substrates: relative substrate activity toward a variety of nucleoside di- and triphosphate substrates
Products: -
Products: -
?
UDP + H2O
UMP + phosphate
-
Substrates: 0.5 mM, 32% relative activity compared to CTP, 8.2% relative activity towards UMP compared to CTP
Products: -
Products: -
?
UDP + H2O
UMP + phosphate
Substrates: relative low substrate activity
Products: -
Products: -
?
UTP + H2O
UDP + phosphate
-
Substrates: 0.5 mM, 66% relative activity compared to CTP
Products: -
Products: -
?
UTP + H2O
UDP + phosphate
Substrates: relative low substrate activity
Products: -
Products: -
?
UTP + H2O
UDP + phosphate
Substrates: -
Products: -
Products: -
?
UTP + H2O
UDP + phosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in RNA replication and capping, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: multifunctional protein, possessing protease, NTPase and helicase activities. These activities are essential for the virus life cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the ATPase activity of NPH I requires single-stranded DNA (ssDNA) as a cofactor. The source of the ssDNA cofactor for NPH I is the upstream portion of the non-template strand in the transcription bubble. In contrast, ssRNA binds to NPH I, but it does not activate ATPase activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
K+
Mg2+
Mn2+
Na+
NaCl
NH4+
Zn2+
additional information
Ca2+
Sc4828 possesses three Ca2+ ions, which all interact with the phosphate group of GDP analog GPCP
Co2+
lower activity in presence of Co2+ than in presence of Mn2+
Mg2+
highest value for Mg2+ requirement in metal profile determined
Mg2+
-
strictly dependent on, coordination of Mg2+ by the Walker B motif, required for all three activities, the RNA helicase, nucleotide 5'-triphosphatase, and RNA 5'-triphosphatase activity
Mg2+
can partially substitute for Mn2+. At the physiological concentration of 1 mM of Mg2+, Ntdp can successfully hydrolyze substrates in vitro
Mg2+
-
required. 150% of the control at an optimum Mg2+ concentration of 1-3 mM
Mn2+
activates, 3.5-5 mM MnCl2 are optimal at an ATP concentration of 0.5 mM
Mn2+
in vitro, highest activity in presence of Mn2+, assay at 10 mM. The physiological concentration of Mn2+ ion, about 0.01 ppb, is too low to promote the hydrolysis process
additional information
-
cation binding to Mg2+-NTP complexes in water, molecular dynamics simulations, overview. Cation binding induces eclipsed conformation of the phosphate chain. Activation of P-loop NTPases by monovalent cations
additional information
-
cation binding to Mg2+-NTP complexes in water, molecular dynamics simulations, overview. Cation binding induces eclipsed conformation of the phosphate chain. Activation of P-loop NTPases by monovalent cations
additional information
-
the enzyme activity depends on divalent cations and prefers Mg2+, Ca2+, and Mn2+
additional information
poor activation by Cu2+, Cd2+, Co2+, and Zn2+, no activation by Ni2+
additional information
-
poor activation by Cu2+, Cd2+, Co2+, and Zn2+, no activation by Ni2+
additional information
no hydrolysis activity is detected under Cu2+ and Zn2+ ion addition
additional information
cations are required for catalytic activity, highest activity with a combination of K+, Mg2+, and Ca2+, with sucrose and glucose
additional information
-
cations are required for catalytic activity, highest activity with a combination of K+, Mg2+, and Ca2+, with sucrose and glucose
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4,5-dihydro-8H-6-(N-decyl)amino-1-(beta-D-ribofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
IC50: 30-100 mg/l
4,5-dihydro-8H-6-(N-dodecyl)amino-1-(beta-D-ribofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
IC50: 1-3 mg/l
4,5-dihydro-8H-6-(N-dodecylamino)-1-(2'-deoxy-alpha-D-erythropentofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
IC50: 3-10 mg/l
4,5-dihydro-8H-6-(N-dodecylamino)-1-(2'-deoxy-beta-D-erythropentofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
IC50: 3-10 mg/l
4,5-dihydro-8H-6-(N-hexadecyl)amino-1-(beta-D-ribofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
IC50: 250 mg/l
4,5-dihydro-8H-6-(N-octadecyl)amino-1-(beta-D-ribofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
IC50: 5.0 mg/l
4,5-dihydro-8H-6-(N-tetradecyl)amino-1-(beta-D-ribofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
IC50: 3-10 mg/l
5-fluoro-2-selenocytosine
-
IC50: 0.075 mM for NTPase reaction, no influence to helicase activity up to a concentration of 0.5 mM
HOCl
-
inhibits the muclear NTPase, taurine acts as antagonist and reduces the hypochlorous acid toxicity
O6-benzyl-N7-chloroethylguanine
-
weak inhibition of NTPase activity, enhances helicase activity
propionate
-
39% relative activity at a concentration of 0.5 mM, 63% relative activity at a concentration of 0.05 mM
ribavirin-TP
-
at ATP concentration equal to Km, IC50 of NTPase reaction is 0.4 mM, classical competitive inhibitor with regard to ATP. At ATP and DNA duplex concentrations corresponding to their KM-values an IC50 of 0.12 mM is measured. Inhibition reaches a maximum of 30% of the control at 0.45 mM and is not competitive with regard to ATP
additional information
-
inhibitor cytotoxicity study, overview
-
additional information
-
a polyclonal immune serum produced against the anti-r-pot B domain, also produced against synthetic peptides LbB1LJ and LbB2LJ derived from this domain, recognizes specifically the B domain of NTPDase 1. The polyclonal antibodies have effective antileishmanial effect, reducing significantly in vitro promastigotes growth by 21-25%. An antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides, potB1LJ and potB2LJ
-
additional information
transcript release is inhibited when the non-template strand of DNA is removed from the transcription bubble
-
additional information
-
the ATPase domain of Cdc6-3, although having lost much of its DNA-binding activity from the origin, inhibits both Cdc6-1 and Cdc6-2
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
stimulating in physiological concentrations, 148% relative activity at a concentration of 0.5 mM, 128% relative activity at a concentration of 0.05 mM
4,5-dihydro-8H-6-(N-phenyl)amino-1-(beta-D-ribofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
activates
acetyl-CoA
-
stimulating in physiological concentrations, 148% relative activity at a concentration of 0.5 mM, 127% relative activity at a concentration of 0.05 mM
D-fructose 1,6-bisphosphate
-
stimulating in physiological concentrations, 155% relative activity at a concentration of 0.5 mM, 126% relative activity at a concentration of 0.05 mM
O6-benzyl-N7-chloroethylguanine
-
weak inhibition of NTPase activity, enhances helicase activity up to 850% of control
O6-benzyl-N9-chloroethylguanine
-
stimulates NTPase activity with a maximum effect of 350% of control at 0.65 mM, enhances helicase activity up to 220% of control
Poly(A)
-
stimulates the ATP hydrolysis dependent on the chain length, highest activation by poly(A)40 comapred to shorter molecules
taurine
-
activates the enzyme, and acts as antagonist and reduces the hypochlorous acid toxicity
additional information
-
activation mechanism, overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site
-
additional information
-
activation mechanism, overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site
-
additional information
ssRNA binds to NPH I, but it does not activate ATPase activity
-
additional information
-
the ATPase domain of Cdc6-2 retains to a great extent the origin DNA-binding activity, and likewise maintains its stimulating effect on Cdc6-3, the ATPase domain of Cdc6-1, which also stimulated the DNA-binding ability of Cdc6-3
-
additional information
-
Rad55B is induced by UV light. Rad55B has a very weak ATPase activity which is not stimulated by DNA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
2',3'-didehydro-thymidine triphosphate
-
pH 7.5, 25°C, NTP hydrolysis-dependent helicase activity
2.3
3'-azido-2',3'-dideoxythymidine triphosphate
-
pH 7.5, 25°C, NTP hydrolysis-dependent helicase activity
0.145
dADP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.092
dCDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.051
dGDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.088
dITP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.092
GDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.046
IDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.105
TDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.137
UDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.217
ADP
substrate concentration between 0.01 and 4.0 mM, 37°C
1.04
ADP
pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose
0.0746
ATP
N45A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.2425
ATP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.317
ATP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.38
ATP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.5158
ATP
mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.8844
ATP
mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
1.26
ATP
pH 7.5, 25°C, recombinant enzyme, in absence of cations
1.53
ATP
pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose
0.082
CDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.034
CTP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.062
dATP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.023
dCTP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.083
dGTP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.077
GTP
mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.0847
GTP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.394
GTP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.6384
GTP
mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
1.2
GTP
pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose
0.147
ITP
substrate concentration between 0.01 and 4.0 mM, 37°C
1.08
ITP
pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose
0.138
TTP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.124
UTP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.55
UTP
pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose
additional information
additional information
steady-state kinetics, Vmax values, overview
-
additional information
additional information
-
steady-state kinetics, Vmax values, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.67
CDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.52
dADP
substrate concentration between 0.01 and 4.0 mM, 37°C
1.12
dCDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.51
dGDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.22
dITP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.39
GDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.06
IDP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.18
ITP
substrate concentration between 0.01 and 4.0 mM, 37°C
1.03
TDP
substrate concentration between 0.01 and 4.0 mM, 37°C
1.35
UDP
substrate concentration between 0.01 and 4.0 mM, 37°C
additional information
additional information
-
at optimum Mg2+ and saturating ATP concentrations 1 pmol of enzyme unwinds 5.5 fmol of DNA duplex per s
-
0.29
ADP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.018
ATP
mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.1333
ATP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.29
ATP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.333
ATP
N45A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.567
ATP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.623
ATP
mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.7
ATP
mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
4.45
ATP
N45A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
155
ATP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)
4384
ATP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)
0.59
CTP
substrate concentration between 0.01 and 4.0 mM, 37°C
220
CTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)
2286
CTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)
0.31
dATP
substrate concentration between 0.01 and 4.0 mM, 37°C
208
dATP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)
3150
dATP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)
0.3
dCTP
substrate concentration between 0.01 and 4.0 mM, 37°C
135
dCTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)
5096
dCTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)
0.4
dGTP
substrate concentration between 0.01 and 4.0 mM, 37°C
136
dGTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)
2500
dGTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)
82
dUTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)
1875
dUTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)
0.012
GTP
mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.033
GTP
mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.32
GTP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.517
GTP
mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
1.733
GTP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
400
GTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)
2963
GTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)
0.69
TTP
substrate concentration between 0.01 and 4.0 mM, 37°C
0.53
UTP
substrate concentration between 0.01 and 4.0 mM, 37°C
114
UTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)
2162
UTP
-
pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.033
ATP
mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.55
ATP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.7
ATP
mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
1.483
ATP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
4.45
ATP
N45A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.15
GTP
mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
0.517
GTP
mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
20.633
GTP
wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
2',3'-didehydro-thymidine triphosphate
-
pH 7.5, 25°C, inhibition of ATPase activity
2.5
2',3'-dideoxy-5-fluorocytidine triphosphate
-
pH 7.5, 25°C, inhibition of ATPase activity
2.1
3'-azido-2',3'-dideoxythymidine triphosphate
-
pH 7.5, 25°C, inhibition of ATPase activity
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.075
5-fluoro-2-selenocytosine
West Nile virus
-
IC50: 0.075 mM for NTPase reaction, no influence to helicase activity up to a concentration of 0.5 mM
0.12
ribavirin-TP
West Nile virus
-
at ATP concentration equal to Km, IC50 of NTPase reaction is 0.4 mM, classical competitive inhibitor with regard to ATP. At ATP and DNA duplex concentrations corresponding to their KM-values an IC50 of 0.12 mM is measured. Inhibition reaches a maximum of
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
dependence on bivalent cations and broad substrate specificity towards nucleoside-5'-tri- and -diphosphates reveal similarities to apyrases
additional information
identification of residues involved in metal and substrate binding using NMR chemical shift mapping experiments, results mapped onto the crystal structure, substrate binding possibilities and biological function discussed, further biochemical studies necessary to determine if the specificity for CDP and CTP is part of its housekeeping duties
additional information
-
identification of residues involved in metal and substrate binding using NMR chemical shift mapping experiments, results mapped onto the crystal structure, substrate binding possibilities and biological function discussed, further biochemical studies necessary to determine if the specificity for CDP and CTP is part of its housekeeping duties
additional information
-
the RNA helicase, nucleotide 5'-triphosphatase, and RNA 5'-triphosphatase activities of wild-type andmutant enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
pH 6.0: about 55% of maximal activity, pH 8.5: about 55% of maximal activity
6.8 - 8
pH 6.8: about 90% of maximal activity, pH 8.0: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
37
44
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 45
at 10°C the enzyme shows little activity, which increases exponentially showing an optimum of 32°C, followed by rapidly decreasing rates and almost null activities at temperatures greater than 45°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
maintained in human foreskin fibroblast (HFF) cell monolayers in regular growth media
brenda
additional information
additional information
-
the transcriptase cofactor my2 is associated to microtubules in host cells, overview
brenda
additional information
-
the transcriptase cofactor my2 is associated to microtubules in host cells, overview
-
brenda
additional information
Vaccinia virions are purified from infected HeLa cells
brenda
additional information
Orthopoxvirus vaccinia Western Reserve
-
Vaccinia virions are purified from infected HeLa cells
-
brenda
additional information
viral protein is expressed in Escherichia coli cells
brenda
additional information
-
viral protein is expressed in Escherichia coli cells
brenda
additional information
-
virus from Vero E6 cell culture, excreted to the medium
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme contains two membrane-spanning helices inserted into the N-terminal Walker B motif
brenda
-
the enzyme contains two membrane-spanning helices inserted into the N-terminal Walker B motif
brenda
-
the enzyme contains two membrane-spanning helices inserted into the N-terminal Walker B motif
brenda
-
the enzyme contains two membrane-spanning helices inserted into the N-terminal Walker B motif
brenda
-
the enzyme contains two membrane-spanning helices inserted into the N-terminal Walker B motif
brenda
-
the enzyme contains two membrane-spanning helices inserted into the N-terminal Walker B motif
brenda
-
the enzyme contains two membrane-spanning helices inserted into the N-terminal Walker B motif
brenda
the enzyme is a membrane bound protein facing the extracellular side of the cell
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism, overview
evolution
-
evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism, overview
evolution
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
evolution
-
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. The sequential hydrolysis of extracellular ATP to adenosine indicates that not only E-NTPDase but also 5'-nucleotidases are present in the plasma membrane. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
evolution
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
evolution
Sequence similarity analysis and distance tree show high level (98%) of identity between Trypanosoma evansi and Trypanosoma brucei brucei (UniProt ID D6XLB5) NTPDase. Trypanosoma evansi NTPDase encloses the GDA1/CD39 nucleoside phosphatase family domain as well as exopolyphosphatase (Ppx-GppA) domain following five apyrase conserved regions (ACR)
evolution
enzyme NPH I is a member of the DEXH box helicase family
evolution
-
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
-
evolution
-
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
-
evolution
Orthopoxvirus vaccinia Western Reserve
-
enzyme NPH I is a member of the DEXH box helicase family
-
malfunction
knockouts of isozymes NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. The NTPase I knockout in the type I strain mirrors the less inhibitory phenotype of type II (ME49) and III (CTG) strains, which naturally lack NTPase I
malfunction
knockouts of isozymes NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. In contrast to the NTPase I mutant, deletion of NTPase II causes only a mild change in inhibition of the FLUC activity in both HeLa cells and RAW-264.7 macrophages
malfunction
-
mutation of the conserved NTPase motifs blocks enzyme activity and viral replication in cells. The RNA destabilization activity is not affected by mutagenesis of the conserved motifs of NTPase
malfunction
simultaneous mutations of the D1 and D2 active-site motifs are required to abolish ATPase activity. ATPase activity is effaced by mutation of the putative D2 arginine finger, suggesting that Msm0858 might oligomerize during the ATPase reaction cycle. A truncated variant Msm0858 (amino acids 212-745) that lacks the N domain is characterized as a catalytically active homodimer
malfunction
-
simultaneous mutations of the D1 and D2 active-site motifs are required to abolish ATPase activity. ATPase activity is effaced by mutation of the putative D2 arginine finger, suggesting that Msm0858 might oligomerize during the ATPase reaction cycle. A truncated variant Msm0858 (amino acids 212-745) that lacks the N domain is characterized as a catalytically active homodimer
-
malfunction
-
simultaneous mutations of the D1 and D2 active-site motifs are required to abolish ATPase activity. ATPase activity is effaced by mutation of the putative D2 arginine finger, suggesting that Msm0858 might oligomerize during the ATPase reaction cycle. A truncated variant Msm0858 (amino acids 212-745) that lacks the N domain is characterized as a catalytically active homodimer
-
physiological function
strong negative influence of NTPase I on the FLUC activity in both HeLa cells and RAW-264.7 macrophages
physiological function
bacterial DExH-box proteins play important roles as co-/posttranscriptional gene regulators, aiding in the adaptation of bacteria to stress conditions. HrpB does not affect curli and biofilm formation in Escherichia coli K-12
physiological function
in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
physiological function
-
in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
physiological function
in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
physiological function
nucleoside triphosphate diphospho-hydrolases (NTPDases) catalyze the hydrolysis of several nucleosides tri and diphosphate playing major roles in eukaryotes including purinergic signaling, inflammation, hemostasis, purine salvage and host-pathogen interactions
physiological function
-
in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
-
physiological function
-
in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
-
additional information
-
combined comparative structure analysis with molecular dynamics simulations of Mg-ATP and Mg-GTP complexes in water and in the presence of potassium, sodium, or ammonium ions. In all analyzed structures of diverse P-loop NTPases, the conserved P-loop motif keeps the triphosphate chain of bound NTPs (or their analogues) in an extended, catalytically prone conformation, similar to that imposed on NTPs in water by potassium or ammonium ions. Mg-NTP complexes and their binding in the active sites of P-loop NTPases, substrate binding, structure overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site. Some P-loop NTPases functionally depend not on Arg/Lys fingers, but on monovalent cations. Molecular dynamics simulations, overview
additional information
-
combined comparative structure analysis with molecular dynamics simulations of Mg-ATP and Mg-GTP complexes in water and in the presence of potassium, sodium, or ammonium ions. In all analyzed structures of diverse P-loop NTPases, the conserved P-loop motif keeps the triphosphate chain of bound NTPs (or their analogues) in an extended, catalytically prone conformation, similar to that imposed on NTPs in water by potassium or ammonium ions. Mg-NTP complexes and their binding in the active sites of P-loop NTPases, substrate binding, structure overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site. Some P-loop NTPases functionally depend not on Arg/Lys fingers, but on monovalent cations. Molecular dynamics simulations, overview
additional information
crystal structure analysis, detailed overview. A globular head is composed of dual RecA, winged-helix, helical bundle and oligonucleotide/oligosaccharide-binding domains, resembling a compact version of eukaryotic DExH-box proteins. Additionally, HrpB harbors a C-terminal region not found in proteins with known structure, which bestows the protein with unique interaction potential. The protein binds RNA but not DNA, hydrolyzes all nucleoside triphosphates in an RNA-stimulated manner, but does not unwind diverse model RNAs in vitro. The entire structure can be divided into seven domains or regions, i.e., two RecA-like domains (RecA1, residues 1-178, and RecA2, residues 179-355), a WH domain (residues 356-416), an HB domain (residues 417-498), an OB domain (residues 499-566), a connector element (CON, residues 567-602) and a C-terminal region (CTR, residues 603-805). The RecA1, RecA2, WH, HB, and OB domains are arranged in a circular fashion, forming the head module, while the remainder of the protein, CON and CTR, forms the C-terminal stalk. Structure comparisons
additional information
-
crystal structure analysis, detailed overview. A globular head is composed of dual RecA, winged-helix, helical bundle and oligonucleotide/oligosaccharide-binding domains, resembling a compact version of eukaryotic DExH-box proteins. Additionally, HrpB harbors a C-terminal region not found in proteins with known structure, which bestows the protein with unique interaction potential. The protein binds RNA but not DNA, hydrolyzes all nucleoside triphosphates in an RNA-stimulated manner, but does not unwind diverse model RNAs in vitro. The entire structure can be divided into seven domains or regions, i.e., two RecA-like domains (RecA1, residues 1-178, and RecA2, residues 179-355), a WH domain (residues 356-416), an HB domain (residues 417-498), an OB domain (residues 499-566), a connector element (CON, residues 567-602) and a C-terminal region (CTR, residues 603-805). The RecA1, RecA2, WH, HB, and OB domains are arranged in a circular fashion, forming the head module, while the remainder of the protein, CON and CTR, forms the C-terminal stalk. Structure comparisons
additional information
-
MNV NS3 has three domains: the N-terminal domain (NTD, 1-105) with a linker (106-129), the core domain (130-285) and the C-terminal domain (CTD, 290-364). The conserved motifs are crucial to the NTPase activity of NS3
additional information
mutational analysis of the A-box and B-box motifs indicated that the D1 and D2 AAA domains are both capable of ATP hydrolysis, structure comparisons of the enzymes with mammalian protein p97, homology of the tandem AAA domains of Msm0858 and p97, overview
additional information
-
mutational analysis of the A-box and B-box motifs indicated that the D1 and D2 AAA domains are both capable of ATP hydrolysis, structure comparisons of the enzymes with mammalian protein p97, homology of the tandem AAA domains of Msm0858 and p97, overview
additional information
-
antibodies against B domain recognize Leishmania infantum promastigote NTPDase 1 and have in vitro antileishmanial activity. IgG1 and IgG2 subclasses binding-epitopes within B domain, IgG1 and IgG2 seropositivity for r-pot B domain recombinant polypeptide, overview
additional information
the binding pocket of Ntdp is composed of divalent metal ions and surrounding amino acid residues (including His25, Arg26, Asn90, Asp110, Asp123, and Glu126). When the substrate coordinates two divalent metal ions through the terminal phosphonate group, Asp106 activates a water molecule as a base to promote a nucleophilic attack on the phosphorus atom of the phosphonate group. The metal ion activates the phosphonate as a Lewis acid, and then, the P-O-P bond in the substrate is cleaved. Residue Arg26 acts as proton source
additional information
-
mutational analysis of the A-box and B-box motifs indicated that the D1 and D2 AAA domains are both capable of ATP hydrolysis, structure comparisons of the enzymes with mammalian protein p97, homology of the tandem AAA domains of Msm0858 and p97, overview
-
additional information
-
mutational analysis of the A-box and B-box motifs indicated that the D1 and D2 AAA domains are both capable of ATP hydrolysis, structure comparisons of the enzymes with mammalian protein p97, homology of the tandem AAA domains of Msm0858 and p97, overview
-
additional information
-
the binding pocket of Ntdp is composed of divalent metal ions and surrounding amino acid residues (including His25, Arg26, Asn90, Asp110, Asp123, and Glu126). When the substrate coordinates two divalent metal ions through the terminal phosphonate group, Asp106 activates a water molecule as a base to promote a nucleophilic attack on the phosphorus atom of the phosphonate group. The metal ion activates the phosphonate as a Lewis acid, and then, the P-O-P bond in the substrate is cleaved. Residue Arg26 acts as proton source
-
additional information
Leishmania infantum MHOM/BR/1972/BH46
-
antibodies against B domain recognize Leishmania infantum promastigote NTPDase 1 and have in vitro antileishmanial activity. IgG1 and IgG2 subclasses binding-epitopes within B domain, IgG1 and IgG2 seropositivity for r-pot B domain recombinant polypeptide, overview
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
60000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 65000, recombinant His-tagged enzyme, SDS-PAGE, x * 65599, sequence calculation
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
RNA helicase, nucleotide 5'-triphosphatase, and RNA 5'-triphosphatase activities are located on the C-terminal 54-kDa domain, the RTPase activity requuires an intact Walker B motif in the helicase core
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
three-dimensional structure determination by NMR and MALDI-TOF mass spectrometry, and structure analysis. The structure of the protein in its complex with ATPgammaS forms a three-layered alpha/beta sandwich, with a central nine-stranded beta-sheet surrounded by five alpha-helices. Sequence and three-dimensional structure comparisons with AAA+ ATPases revealed the presence of Walker A, GPPGVGKT, and Walker B, VCVIDEIG, motifs, overview
additional information
-
the enzyme contains an N-terminal zinc binding domain and a C-terminal superfamily 1 helicase domain
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
-
additional information
-
MNV NS3 has three domains: the N-terminal domain (NTD, 1-105) with a linker (106-129), the core domain (130-285) and the C-terminal domain (CTD, 290-364)
additional information
-
the enzyme contains a leucine-rich repeat-replete, LRR-replete, conserved in NACHT NTPases, three-dimensional structure
additional information
the Msm0858 structure comprises (i) an N-terminal domain (amino acids 17-201) composed of two beta-barrel modules and (ii) two AAA domains, D1 (amino acids 212-473) and D2 (amino acids 476-744), each of which has ADP in the active site. Msm0858-ADP is a monomer in solution and in crystallized form. The D1 and D2 AAA domains are both capable of ATP hydrolysis, Enzyme structure analysis, detailed overview. Msm0858 might oligomerize during the ATPase reaction cycle
additional information
-
the Msm0858 structure comprises (i) an N-terminal domain (amino acids 17-201) composed of two beta-barrel modules and (ii) two AAA domains, D1 (amino acids 212-473) and D2 (amino acids 476-744), each of which has ADP in the active site. Msm0858-ADP is a monomer in solution and in crystallized form. The D1 and D2 AAA domains are both capable of ATP hydrolysis, Enzyme structure analysis, detailed overview. Msm0858 might oligomerize during the ATPase reaction cycle
additional information
-
the Msm0858 structure comprises (i) an N-terminal domain (amino acids 17-201) composed of two beta-barrel modules and (ii) two AAA domains, D1 (amino acids 212-473) and D2 (amino acids 476-744), each of which has ADP in the active site. Msm0858-ADP is a monomer in solution and in crystallized form. The D1 and D2 AAA domains are both capable of ATP hydrolysis, Enzyme structure analysis, detailed overview. Msm0858 might oligomerize during the ATPase reaction cycle
-
additional information
-
the Msm0858 structure comprises (i) an N-terminal domain (amino acids 17-201) composed of two beta-barrel modules and (ii) two AAA domains, D1 (amino acids 212-473) and D2 (amino acids 476-744), each of which has ADP in the active site. Msm0858-ADP is a monomer in solution and in crystallized form. The D1 and D2 AAA domains are both capable of ATP hydrolysis, Enzyme structure analysis, detailed overview. Msm0858 might oligomerize during the ATPase reaction cycle
-
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the type IV pilus motor proteins contain conserved residues in the Walker A, Walker B, and Asp Box and His Box motifs characteristic of secretion NTPases, overview
additional information
-
the type IV pilus motor proteins contain conserved residues in the Walker A, Walker B, and Asp Box and His Box motifs characteristic of secretion NTPases, overview
-
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
additional information
-
the enzyme has the conserved P-loop NTPase fold, amino acid sequence alignment and structure comparison of KAP NTPases, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determined in the metal-free form at 1.9 A resolution, data collection and structure refinement statistics, molscript ribbon representation of the crystal structure
purified recombinant selenomethionine-derivatized full-length enzyme, X-ray diffraction structrue determination and analysis. The final model of HrpBFL contains residues 1-805 without gaps and three additional residues (Ala-Met-Ala) at the N terminus that remained after tag cleavage. The overall structure of HrpBFL resembles a mushroom with a globular head module (residues 1-566) and an extended stalk (residues 567-805)
purified recombinant wild-type enzyme and SeMet-labeled enzyme, hanging drop vapor diffusion method, mixing of 6.5 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, and 10 mM DTT, with an equal volume of reservoir solution containing 0.3 M ammonium tartrate dibasic and 25% PEG 3350, room temperature, 1 week, X-ray diffraction structure determination and analysis at 2.5 and 3.2 A resolution, respectively
sitting drop vapor diffusion method, using 8-10% (w/v) PEG 3350, 0.1 M Tris-HCl pH 7.4, 50 mM diammonium phosphate and 2%(v/v) glycerol, at 20°C
structures of apo-Ntdp and in complex with substrate analogues ATPgammaS, GDPbetaS, and GTPgammaS
sitting drop vapor diffusion method, using 10-12% (w/v) PEG 3350, 0.1 M Tris-HCl pH 7.4, 2% (v/v) glycerol, at 20°C
structures of apo-Ntdp and in complex with substrate analogues ATPgammaS, GDPbetaS, and GTPgammaS
structures of apo-Ntdp and in complex with substrate analogues ATPgammaS, GDPbetaS, and GTPgammaS
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A354V
-
site-directed mutagenesis of the motif III residue does not affect the enzyme activity and kinetics
K232A
-
site-directed mutagenesis of the conserved motif I residue leads to inactivation of the mutant
A354V
-
site-directed mutagenesis of the motif III residue does not affect the enzyme activity and kinetics
-
K232A
-
site-directed mutagenesis of the conserved motif I residue leads to inactivation of the mutant
-
D284A
-
site-directed mutagenesis, mutation in the Walker B motif, inactive mutant
E285A
-
site-directed mutagenesis, mutation in the Walker B motif, the mutant does not show RTPase and NTPase activities, and is unable to remove gamma-phosphate from substrate pppAC5
E578A
-
site-directed mutagenesis, mutation of a highly conserved residue, the mutant retains full NTPase, RTPase and helicase activities
K199A
-
site-directed mutagenesis, mutation in the Walker B motif, the mutant does not show RTPase and NTPase activities, and is unable to remove gamma-phosphate from substrate pppAC5
R513A
-
site-directed mutagenesis, mutation in the C-terminal domain of DELTANS3, the mutation reduces NTPase activity, abrogates helicase activity and strongly diminishes RTPase activity
E113T
-
site-directed mutagenesis, the mutation in the NTP binding site has a significant effect on the hydrolysis rate of the purine nucleotides, but has only a small effect on the protein structure
G115H
-
site-directed mutagenesis, the mutation in the NTP binding site has a significant effect on the hydrolysis rate of the purine nucleotides, but has only a small effect on the protein structure
K415A/K419A
D213A
-
site-directed mutagenesis, mutant shows significantly reduced NTPase activity compared to the wild-type NS3 protein
K169A
-
site-directed mutagenesis, the mutant shows significantly reduced NTPase activity compared to the wild-type NS3 protein
N260A
-
site-directed mutagenesis, mutant shows significantly reduced NTPase activity compared to the wild-type NS3 protein
D327A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E585A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
K276A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
K532A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
R641A
site-directed mutagenesis, Arg641 is the predicted arginine finger of the D2 AAA domain based on the structural alignment of Msm0858 to p97, almost inactive mutant
D327A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
E585A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
K276A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
K532A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
D327A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
E585A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
K276A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
K532A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
D160N
-
site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
E159Q
-
site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
E163Q
-
site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
E204Q
-
site-directed mutagenesis, mutation of the Walker B motif residue in PilT
G135S
-
site-directed mutagenesis, mutation of the Walker A motif residue in PilT
H222A
-
site-directed mutagenesis, mutation of the His Box motif residue in PilT
H229A
-
site-directed mutagenesis, mutation of the His Box motif residue in PilT
D160N
-
site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
-
E159Q
-
site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
-
E163Q
-
site-directed mutagenesis, mutation of the Asp Box motif residue in PilT
-
E204Q
-
site-directed mutagenesis, mutation of the Walker B motif residue in PilT
-
G135S
-
site-directed mutagenesis, mutation of the Walker A motif residue in PilT
-
Y88A
Kcat/Km value decreases about 28fold compared with wild-type
N45A
mutation eliminates the hydrolysis activity of Ntdp to GTP
Y88A
Kcat/Km value decreases about 28fold compared with wild-type
D106A
-
mutation eliminates activity on ATP, ADT, GTP, and GDP
-
D108A
-
mutation eliminates activity on ATP, ADT, GTP, and GDP
-
D110A
-
mutation eliminates activity on ATP, ADT, GTP, and GDP
-
D123A
-
mutation eliminates activity on ATP, ADT, GTP, and GDP
-
N90A
-
mutation eliminates activity on ATP, ADT, GTP, and GDP
-
additional information
K415A/K419A
-
site-directed mutagenesis, mutation of residues in the nucleotide binding domain of transcriptase cofactor my2, leads to loss of enzyme activity
K415A/K419A
-
site-directed mutagenesis, mutation of residues in the nucleotide binding domain of transcriptase cofactor my2, leads to loss of enzyme activity
-
additional information
-
construction of mutant DELTANS3 comprising the C-terminal 54-kDa domain of NS3, amino acid residues 169-619
additional information
construction and comparative phenotypic analyses of a hrpB knockout mutants, overview
additional information
-
construction and comparative phenotypic analyses of a hrpB knockout mutants, overview
additional information
-
site-directed mutagenesis of the conserved NTPase motifs in NS3 blocking enzyme activity and viral replication in cells
additional information
construction of a truncated variant Msm0858 (amino acids 212-745) that lacks the N domain, the mutant is a catalytically active homodimer, quarternary strutcure analysis, overview
additional information
-
construction of a truncated variant Msm0858 (amino acids 212-745) that lacks the N domain, the mutant is a catalytically active homodimer, quarternary strutcure analysis, overview
additional information
-
construction of a truncated variant Msm0858 (amino acids 212-745) that lacks the N domain, the mutant is a catalytically active homodimer, quarternary strutcure analysis, overview
-
additional information
-
construction of a truncated variant Msm0858 (amino acids 212-745) that lacks the N domain, the mutant is a catalytically active homodimer, quarternary strutcure analysis, overview
-
additional information
-
virus C-terminal regions deletion diminishes the ATPase activity
additional information
-
mutation of conserved Walker A or Walker B residues in any of the three ATPases abrogates twitching motility, and for the Walker A mutant of PilT causes loss of polar localization, construction of diverse mutants of the type IV pilus motor proteins, overview
additional information
targeted gene disruption of gene sso0909 via genetic recombination, mutant phenotype, overview
additional information
-
targeted gene disruption of gene sso0909 via genetic recombination, mutant phenotype, overview
additional information
generation of NTPase single- and double-disruptant mutants using CRISPR/Cas9 technology, the disruptant mutants lack either NTPase I (DELTAntpase I, RHDELTAhxgprt/ntpaseI::DHFR) or NTPase II (DELTAntpase II, RHDELTAhxgprt/ntpaseII::DHFR) or both. Knockouts of NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. Toxoplasma gondii strains null for both NTPase I and NTPase II can be used to avoid interference artifacts in ATP-dependent assays
additional information
generation of NTPase single- and double-disruptant mutants using CRISPR/Cas9 technology, the disruptant mutants lack either NTPase I (DELTAntpase I, RHDELTAhxgprt/ntpaseI::DHFR) or NTPase II (DELTAntpase II, RHDELTAhxgprt/ntpaseII::DHFR) or both. Knockouts of NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. Toxoplasma gondii strains null for both NTPase I and NTPase II can be used to avoid interference artifacts in ATP-dependent assays
additional information
-
generation of NTPase single- and double-disruptant mutants using CRISPR/Cas9 technology, the disruptant mutants lack either NTPase I (DELTAntpase I, RHDELTAhxgprt/ntpaseI::DHFR) or NTPase II (DELTAntpase II, RHDELTAhxgprt/ntpaseII::DHFR) or both. Knockouts of NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. Toxoplasma gondii strains null for both NTPase I and NTPase II can be used to avoid interference artifacts in ATP-dependent assays
additional information
generation of NTPase single- and double-disruptant mutants using CRISPR/Cas9 technology, the disruptant mutants lack either NTPase I (DELTAntpase I, RHDELTAhxgprt/ntpaseI::DHFR) or NTPase II (DELTAntpase II, RHDELTAhxgprt/ntpaseII::DHFR) or both. Knockouts of NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. ATP-dependent assays
additional information
generation of NTPase single- and double-disruptant mutants using CRISPR/Cas9 technology, the disruptant mutants lack either NTPase I (DELTAntpase I, RHDELTAhxgprt/ntpaseI::DHFR) or NTPase II (DELTAntpase II, RHDELTAhxgprt/ntpaseII::DHFR) or both. Knockouts of NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. ATP-dependent assays
additional information
-
generation of NTPase single- and double-disruptant mutants using CRISPR/Cas9 technology, the disruptant mutants lack either NTPase I (DELTAntpase I, RHDELTAhxgprt/ntpaseI::DHFR) or NTPase II (DELTAntpase II, RHDELTAhxgprt/ntpaseII::DHFR) or both. Knockouts of NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. ATP-dependent assays
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from virus Vero E6 cell culture medium by affinity chromatography, ultrafiltration, and gel filtration
-
recombinant enzyme from Escherichia coli
recombinant enzyme from Escherichia coli strain HMS174 by streptomycin sulfate treatment and gel filtration
-
recombinant GST-tagged Sso0909 from Escherichia coli by glutathione affinity chromatography and gel filtration, recombinant His10-tagged Sso0909 from Sulfolobus solfataricus by nickel affinity chromatography and gel filtration to homogeneity
recombinant His-tagged DEAH-box Prp22 protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
-
recombinant His-tagged full-length viral NS3 protein and N-terminal truncated version ntNS3 from Escherichia coli by nickel affinity chromatography and dialysis
-
recombinant His6-tagged coat protein from Escherichia coli by nickel affinity chromatogryphy
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain Bl21 by nickel affinity chromatography
-
recombinant MBP-tagged enzyme from Escherichia coli by amylose affinity chromatography and gel filtration. When the MBP-NS3 is treated with TEV protease to remove its MBP tag, the free NS3 becomes unstable and aggregates
-
recombinant soluble His-tagged enzyme from Escherichia coli strain Rosetta Gammi (DE3) to homogeneity by nickel affinity chromatography and dialysis
recombinant wild-type and mutant enzymes from Escherichia coli by cation exchange chromatography and gel filtration to homogeneity
-
recombinant wild-type or SeMet-labeled His10-tagged enzyme from Escherichia coli strains BL21(DE3) or B834 by nickel affinity chromatography, tag cleavage by Smt3-specific protease Ulp1, a second step of nickel affinity chromatography, and ultrafiltration, followed by dialysis
recombinat His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
Toyopearl DEAE-650S column chromatography, Source 15Q column chromatography, and Superdex 200 pg gel filtration
transcriptase cofactor my2 from host nucleoplasma by ion exchange and adsorption chromatography at room temperature
-
recombinant His6-tagged coat protein from Escherichia coli by nickel affinity chromatogryphy
-
recombinant His6-tagged coat protein from Escherichia coli by nickel affinity chromatogryphy
-
Toyopearl DEAE-650S column chromatography, Source 15Q column chromatography, and Superdex 200 pg gel filtration
Toyopearl DEAE-650S column chromatography, Source 15Q column chromatography, and Superdex 200 pg gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli
-
DNA and amino acid sequence determination and analysis, functional expression of His-tagged full-length viral NS3 protein, i.e. NS3FL, and its N-terminal truncated version ntNS3 in Escherichia coli
-
DNA and amino acid sequence determination and analysis, recombinant expression of the soluble His-tagged enzyme in Escherichia coli strain Rosetta Gammi (DE3)
enzyme expression in Escherichia coli
expressed in Escherichia coli BL21 cells
expression in Escherichia coli
expression of His-tagged DEAH-box Prp22 protein in Escherichia coli strain BL21(DE3)
-
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
functional overexpression of the His6-tagged coat protein in Escherichia coli
gene M1, expression of transcriptase cofactor my2 mutant K415A/K419A in Spodoptera frugiperda Sf21 insect cells using the baculovirus system
-
gene MSMEG_0858, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21(DE3) and of selenomethionine (SeMet)-substituted Msm0858 in Escherichia coli strain B834
gene Nalp14, DNA and amino acid sequence determination and analysis, genomic organization and allelic representation, expression analysis, overview, expression of NALP14 in Escherichia coli strain XL-2 Blue
-
gene sso0909, DNA and amino acid sequence determination and analysis, expression analysis, sequence comparisons, phylogenetic analysis, overview. Expression of GST-tagged Sso0909 in Escherichia coli, overexpression of His10-tagged Sso0909 in Sulfolobus solfataricus
gene ytkD, expression in Escherichia coli strain HMS174, complementation of the mutT mutator phenotype in Escherichia coli strain SB3 lacking a functional mutT gene
-
genes pilB, pilT and pilU, DNA and amino acid sequence determination and anaylsis, expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Bl21
-
phylogenetic tree and analysis of KAP NTPases, overview
recombinant expression of C-terminally His-tagged enzyme in Escherichia coli in inclusion bodies, recombinant expression of MBP-tagged enzyme in Escherichia coli
-
sequence comparisons
functional overexpression of the His6-tagged coat protein in Escherichia coli
-
functional overexpression of the His6-tagged coat protein in Escherichia coli
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
considered attractive target for anti-hepatitis C virus chemoterapy
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vianna, A.L.
Interaction of calcium and magnesium in activating and inhibiting the nucleoside triphosphatase of sarcoplasmic reticulum vesicles
Biochim. Biophys. Acta
410
389-406
1975
Oryctolagus cuniculus
-
brenda
Schrder, H.C.; Rottmann, M.; Bachmann, M.; Muller, W.E.G.
Purification and characterization of the major nucleoside triphosphatase from rat liver nuclear envelopes
J. Biol. Chem.
261
663-668
1986
Rattus norvegicus
brenda
Clawson, G.A.; Woo, C.H.; Button, J.; Smuckler, E.A.
Photoaffinity labeling of the major nucleosidetriphosphatase of rat liver nuclear envelope
Biochemistry
23
3501-3507
1984
Rattus norvegicus
brenda
Paoletti, E.; Moos, B.
Two nucleic acid-dependent nucleoside triphosphate phosphohydrolases from vaccinia virus. Nucleotide substrate and polynucleotide cofactor specificities
J. Biol. Chem.
249
3281-3286
1974
Orthopoxvirus vaccinia
brenda
Harper, F.; Lamy, F.; Calvert, R.
Some properties of a Ca2+- and (or) Mg2+-requiring nucleoside di- and tri-phosphatase(s) associated with the membranes of rat pancreatic zymogen granules
Can. J. Biochem.
56
565-567
1978
Rattus norvegicus
brenda
Chen, Y.R.; Roux, S.J.
Characterization of nucleoside triphosphatase activity in isolated pea nuclei and its photoreversible regulation by light
Plant Physiol.
81
609-613
1986
Lathyrus oleraceus
brenda
McCarty, D.R.; Selman, B.
Partial purification of a nucleoside triphosphatase from the inner membrane of the chloroplast envelope of pea
Arch. Biochem. Biophys.
248
523-531
1986
Lathyrus oleraceus
brenda
McCarty, D.R.; Selman, B.
Properties of a partially purified nucleoside triphosphatase (NTPase) from the chloroplast envelope of pea
Plant Physiol.
80
908-912
1986
Lathyrus oleraceus
brenda
Chen, Y.R.; Datta, N.; Roux, S.J.
Purification and partial characterization of a calmodulin-stimulated nucleoside triphosphatase from pea nuclei
J. Biol. Chem.
262
10689-10694
1987
Lathyrus oleraceus
brenda
Plesner L.; Juul B.; Scriver E.; Aalkjaer C.
Characterisation of Ca2+ or Mg2+-dependent nucleoside triphosphatase from rat mesenteric small arteries
Biochim. Biophys. Acta
1067
191-200
1991
Rattus norvegicus
brenda
Pfister T.; Wimmer E.
Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication
J. Biol. Chem.
274
6992-7001
1999
Enterovirus C
brenda
Dahlmann N.; Kirchgesser M.
Acid nucleoside triphosphatase: partial purification and characterization of a new enzyme from human serum
Biochem. Int.
20
317-327
1990
Homo sapiens
brenda
Zhang, N.; Chen, H.M.; Koch, V.; Schmitz, H.; Minczuk, M.; Stepien, P.; Fattom, A.I.; Naso, R.B.; Kalicharran, K.; Borowski, P.; Hosmane, R.S.
Potent inhibition of NTPase/helicase of the West Nile Virus by ring-expanded ("fat") nucleoside analogues
J. Med. Chem.
46
4776-4789
2003
West Nile virus
brenda
Locatelli, G.A.; Gosselin, G.; Spadari, S.; Maga, G.
Hepatitis C virus NS3 NTPase/helicase:different stereoselectivity in nucleoside triphosphate utilisation suggests that NTPase and helicase activities are coupled by a nucleotide-dependent rate limiting step
J. Mol. Biol.
313
683-694
2001
Hepacivirus hominis
brenda
Pfister, T.; Wimmer, E.
Polypeptide p41 of a Norwalk-like virus is a nucleic acid-independent nucleoside triphosphatase
J. Virol.
75
1611-1619
2001
Southampton virus (Q04544), Southampton virus
brenda
Borowski, P.; Niebuhr, A.; Mueller, O.; Bretner, M.; Felczak, K.; Kulikowski, T.; Schmitz, H.
Purification and characterization of West Nile virus nucleoside triphosphatase (NTPase)/helicase: evidence for dissociation of the NTPase and helicase activities of the enzyme
J. Virol.
75
3220-3229
2001
West Nile virus
brenda
Bretner, M.; Baier, A.; Kopanska, K.; Najda, A.; Schoof, A.; Reinholz, M.; Lipniacki, A.; Piasek, A.; Kulikowski, T.; Borowski, P.
Synthesis and biological activity of 1H-benzotriazole and 1H-benzimidazole analogues - inhibitors of the NTPase/helicase of HCV and of some related Flaviviridae
Antiviral Chem. Chemother.
16
315-326
2005
Hepacivirus hominis, West Nile virus, Dengue virus, Japanese encephalitis virus
brenda
Tanaka, N.; Schwer, B.
Characterization of the NTPase, RNA-binding, and RNA helicase activities of the DEAH-box splicing factor Prp22
Biochemistry
44
9795-9803
2005
Saccharomyces cerevisiae
brenda
Horikawa, M.; Kirkman, N.J.; Mayo, K.E.; Mulders, S.M.; Zhou, J.; Bondy, C.A.; Hsu, S.Y.; King, G.J.; Adashi, E.Y.
The mouse germ-cell-specific leucine-rich repeat protein NALP14: a member of the NACHT nucleoside triphosphatase family
Biol. Reprod.
72
879-889
2005
Mus musculus
brenda
Rakitina, D.V.; Kantidze, O.L.; Leshchiner, A.D.; Solovyev, A.G.; Novikov, V.K.; Morozov, S.Y.; Kalinina, N.O.
Coat proteins of two filamentous plant viruses display NTPase activity in vitro
FEBS Lett.
579
4955-4960
2005
potato virus X, potato virus A, no activity in tobacco mosaic virus
brenda
Aravind, A.L.; Lakshminarayan, I.L.; Leipe, D.D.; Koonin, E.V.
A novel family of P-loop NTPases with an unusual phyletic distribution and transmembrane segments inserted within the NTPase domain
Genome Biol.
5
R30
2004
Corynebacterium efficiens, Deinococcus radiodurans, Drosophila melanogaster, Escherichia coli, Geobacter sulfurreducens, Homo sapiens, Klebsiella pneumoniae, Leuconostoc mesenteroides, Magnetococcus sp., Saccharophagus degradans, Nostoc punctiforme, Pseudomonas putida, Cupriavidus metallidurans, Rattus norvegicus, Staphylococcus epidermidis, Synechocystis sp., Thermotoga maritima, Vibrio parahaemolyticus, Vibrio vulnificus, Agrobacterium tumefaciens, Anabaena sp., Caenorhabditis elegans, Corynebacterium glutamicum, Clostridium perfringens, Magnetococcus sp. mc-1
brenda
Xu, W.; Jones, C.R.; Dunn, C.A.; Bessman, M.J.
Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily
J. Bacteriol.
186
8380-8384
2004
Bacillus subtilis, Bacillus subtilis 168
brenda
Kim, J.; Parker, J.S.; Murray, K.E.; Nibert, M.L.
Nucleoside and RNA triphosphatase activities of Orthoreovirus transcriptase cofactor mu2
J. Biol. Chem.
279
4394-4403
2004
mammalian orthoreovirus, mammalian orthoreovirus mORV
brenda
Ivanov, K.A.; Ziebuhr, J.
Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5-triphosphatase activities
J. Virol.
78
7833-7838
2004
Human coronavirus 229E
brenda
Benarroch, D.; Selisko, B.; Locatelli Giada, A.; Maga, G.; Romette, J.L.; Canard, B.
The RNA helicase, nucleotide 5'-triphosphatase, and RNA 5'-triphosphatase activities of Dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core
Virology
328
208-218
2004
Dengue virus
brenda
Li, J.X.; Pang, Y.Z.; Tang, C.S.; Li, Z.Q.
Protective effect of taurine on hypochlorous acid toxicity to nuclear nucleoside triphosphatase in isolated nuclei from rat liver
World J. Gastroenterol.
10
694-698
2004
Rattus norvegicus
brenda
Wen, G.; Chen, C.; Luo, X.; Wang, Y.; Zhang, C.; Pan, Z.
Identification and characterization of the NTPase activity of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) expressed in bacteria
Arch. Virol.
152
1565-1573
2007
Classical swine fever virus, Classical swine fever virus CSFV
brenda
Placzek, W.J.; Almeida, M.S.; Wuethrich, K.
NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase
J. Mol. Biol.
367
788-801
2007
Homo sapiens
brenda
Chiang, P.; Sampaleanu, L.M.; Ayers, M.; Pahuta, M.; Howell, P.L.; Burrows, L.L.
Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU
Microbiology
154
114-126
2008
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAK
brenda
He, Z.G.; Feng, Y.; Wang, J.; Jiang, P.X.
The regulatory function of N-terminal AAA+ ATPase domain of eukaryote-like archaeal Orc1/Cdc6 protein during DNA replication initiation
Arch. Biochem. Biophys.
471
176-183
2008
Saccharolobus solfataricus
brenda
Hobel, C.F.; Albers, S.V.; Driessen, A.J.; Lupas, A.N.
The Sulfolobus solfataricus AAA protein Sso0909, a homologue of the eukaryotic ESCRT Vps4 ATPase
Biochem. Soc. Trans.
36
94-98
2008
Saccharolobus solfataricus (Q97ZJ7), Saccharolobus solfataricus
brenda
Sheng, D.; Li, M.; Jiao, J.; Ni, J.; Shen, Y.
Co-expression with RadA and the characterization of stRad55B, a RadA paralog from the hyperthermophilic crenarchaea Sulfolobus tokodaii
Sci. China C Life Sci.
51
60-65
2008
Sulfurisphaera tokodaii
brenda
Sivuk, V.F.; Rusina, I.M.; Makarchikov, A.F.
Purification and characteristics of functional properties of soluble nucleoside triphosphatase (apyrase) from bovine brain
Biochemistry (Moscow)
73
1047-1052
2008
Bos taurus
brenda
Buchko, G.W.; Litvinova, O.; Robinson, H.; Yakunin, A.F.; Kennedy, M.A.
Functional and structural characterization of DR_0079 from Deinococcus radiodurans, a novel nudix hydrolase with a preference for cytosine (deoxy)ribonucleoside 5-di- and triphosphates
Biochemistry
47
6571-6582
2008
Deinococcus radiodurans (Q9RXX6), Deinococcus radiodurans
brenda
Matoba, K.; Shiba, T.; Takeuchi, T.; Sibley, L.D.; Seiki, M.; Kikyo, F.; Horiuchi, T.; Asai, T.; Harada, S.
Crystallization and preliminary X-ray structural analysis of nucleoside triphosphate hydrolases from Neospora caninum and Toxoplasma gondii
Acta Crystallogr. Sect. F
66
1445-1448
2010
Toxoplasma gondii (Q27893), Neospora caninum (C9K7J7)
brenda
Paes-Vieira, L.; Gomes-Vieira, A.L.; Meyer-Fernandes, J.R.
NTPDase activities possible roles on Leishmania spp. infectivity and virulence
Cell Biol. Int.
42
670-682
2018
Leishmania donovani (E9BA63), Leishmania infantum, Leishmania mexicana (E9AQ00), Leishmania mexicana (E9AN23), Leishmania mexicana MHOM/GT/2001/U1103 (E9AQ00), Leishmania mexicana MHOM/GT/2001/U1103 (E9AN23), Leishmania donovani BPK282A1 (E9BA63)
brenda
Shalaeva, D.N.; Cherepanov, D.A.; Galperin, M.Y.; Golovin, A.V.; Mulkidjanian, A.Y.
Evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism
eLife
7
e37373
2018
Escherichia coli, Arabidopsis thaliana
brenda
Weiss, P.H.; Batista, F.; Wagner, G.; Magalhaes, M.d.e. .L.; Miletti, L.C.
Kinetic and biochemical characterization of Trypanosoma evansi nucleoside triphosphate diphosphohydrolase
Exp. Parasitol.
153
98-104
2015
Trypanosoma evansi (A0A0E3JDD8), Trypanosoma evansi
brenda
Olias, P.; Sibley, L.D.
Functional analysis of the role of Toxoplasma gondii nucleoside triphosphate hydrolases I and II in acute mouse virulence and immune suppression
Infect. Immun.
84
1994-2001
2016
Toxoplasma gondii (Q27893), Toxoplasma gondii (Q27895), Toxoplasma gondii
brenda
Unciuleac, M.C.; Smith, P.C.; Shuman, S.
Crystal structure and biochemical characterization of a Mycobacterium smegmatis AAA-type nucleoside triphosphatase phosphohydrolase (Msm0858)
J. Bacteriol.
198
1521-1533
2016
Mycolicibacterium smegmatis (A0QQS4), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0QQS4), Mycolicibacterium smegmatis mc(2)155 (A0QQS4)
brenda
Hindman, R.; Gollnick, P.
Nucleoside triphosphate phosphohydrolase I (NPH I) functions as a 5 to 3 translocase in transcription termination of vaccinia early genes
J. Biol. Chem.
291
14826-14838
2016
Orthopoxvirus vaccinia (P05807), Orthopoxvirus vaccinia Western Reserve (P05807)
brenda
Han, K.R.; Lee, J.H.; Kotiguda, G.G.; Jung, K.H.; Chung, M.S.; Kang, S.; Hwang, S.; Kim, K.H.
Nucleotide triphosphatase and RNA chaperone activities of murine norovirus NS3
J. Gen. Virol.
99
1482-1493
2018
Murine norovirus
brenda
Pietrzyk-Brzezinska, A.J.; Absmeier, E.; Klauck, E.; Wen, Y.; Antelmann, H.; Wahl, M.C.
Crystal structure of the Escherichia coli DExH-Box NTPase HrpB
Structure
26
1462-1473e4
2018
Escherichia coli (P37024), Escherichia coli
brenda
Maia, A.C.R.G.; Porcino, G.N.; Faria-Pinto, P.; Mendes, T.V.; Antinarelli, L.M.R.; Coimbra, E.S.; Reis, A.B.; Juliano, L.; Juliano, M.A.; Marques, M.J.; Vasconcelos, E.G.
Leishmania infantum nucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) B-domain Antibody antiproliferative effect on the promastigotes and IgG subclass responses in canine visceral leishmaniasis
Vet. Parasitol.
271
38-44
2019
Leishmania infantum, Leishmania infantum MHOM/BR/1972/BH46
brenda
Wang, Z.; Shen, H.; He, B.; Teng, M.; Guo, Q.; Li, X.
The structural mechanism for the nucleoside tri- and diphosphate hydrolysis activity of Ntdp from Staphylococcus aureus
FEBS J.
288
6019-6034
2021
Staphylococcus aureus (Q7A4T2), Streptomyces coelicolor (Q9FBN7), Staphylococcus aureus N315 (Q7A4T2), Streptomyces coelicolor ATCC BAA-471 (Q9FBN7)
brenda
EXTERNAL LINKS (specific for EC-Number 3.6.1.15)
Transporter Classification Database (TCDB): 1.G.3.1.7, 1.A.53.1.5, 1.A.122.1.2, 1.A.53.1.7, 1.A.85.1.7, 1.G.3.1.2, 1.G.3.1.1, 1.A.85.1.4, 1.A.85.1.8, 1.A.53.1.11, 1.A.53.1.6, 1.A.85.1.1
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