Information on EC 3.6.1.3 - adenosinetriphosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.6.1.3
-
RECOMMENDED NAME
GeneOntology No.
adenosinetriphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
(Ca2+-Mg2+)-ATPase: no phosphorylated intermediate formed
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Purine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase
Many enzymes previously listed under this number are now listed separately under EC 3.6.3 and EC 3.6.4.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(Ca2+ + Mg2+)-ATPase
-
-
-
-
ABCA1
-
-
adenosine 5'-triphosphatase
-
-
-
-
adenosine triphosphatase
-
-
-
-
adenosine triphosphatase
-
-
adenylpyrophosphatase
-
-
-
-
Af1285
O28983
gene name
ATP hydrolase
-
-
-
-
ATP monophosphatase
-
-
-
-
ATP-binding cassette protein A1
-
-
ATPase
-
-
-
-
ATPase
-
-
ATPase
-
-
ATPase
Pyrococcus horikoshii OT-3
-
-
-
ATPase SSO1545
Q97Y08
-
ATPase SSO1545
Q97Y08
-
-
Cdc6/Orc1 protein
P81413
-
CHD1L
-
-
chromodomain helicase/adenosine triphosphatase DNA binding protein 1-like protein
-
-
complex V (mitochondrial electron transport)
-
-
-
-
ecto-F1-ATPase
-
-
F1-adenosine triphosphatase
-
-
F1-ATPase
-
-
HCO3--ATPase
-
-
-
-
Hsp70 protein
-
isoforms HSPA1A, HSPA1L, HSPA2, HSPA5, and HSPA6. Hsp70 proteins consist of two major functional domains: an N-terminal nucleotide binding domain with ATPase activity, and a C-terminal substrate binding domain
lambda1 protein
-
-
MBA1
Q97W25
-
-
MBA2
Q97V06
-
-
membrane ATP synthase
-
-
Mg2+-ATPase
-
-
-
-
nucleic acid-independent nucleoside triphosphatase
Q04544
-
nucleoside triphosphatase (NTPase)/helicase
-
-
PABY2304
Q9V2L3
gene name
PH0284
Pyrococcus horikoshii OT-3
-
-
-
PH0284 protein
-
-
PH0284 protein
Pyrococcus horikoshii OT-3
-
-
-
phosphatase, adenosine tri-
-
-
-
-
polypeptide p41
Q04544
-
secretion ATPase
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
-
secretion ATPase
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
-
-
SHVp41
Q04544
-
single-stranded DNA-dependent ATPase
-
-
single-stranded-DNA-stimulated ATPase
Q97ZF9, Q97ZV2
-
single-stranded-DNA-stimulated ATPase
Q97ZF9, Q97ZV2
-
-
ssDNA-dependent ATPase
-
-
SSO0120
Q7LXX6
locus name
SSO0120
Q7LXX6
locus name
-
SSO0473
Q97ZV2
locus name
SSO0473
Q97ZV2
locus name
-
SSO0572
Q7LXU1
locus name
SSO0572
Q7LXU1
locus name
-
SSO0959
Q97ZF9
locus name
SSO0959
Q97ZF9
locus name
-
SSO2387
Q97W53
locus name
SSO2387
Q97W53
locus name
-
SSO2420
Q97W25
locus name
SSO2420
Q97W25
locus name
-
SSO2452
Q97VZ8
locus name
SSO2452
Q97VZ8
locus name
-
SSO2680
Q97VE6
locus name
SSO2680
Q97VE6
locus name
-
SSO2831
Q97V06
locus name
SSO2831
Q97V06
locus name
-
ST0579
F9VN39
locus name
ST0579
Sulfolobus tokodaii 7
F9VN39
locus name
-
stRad55A
F9VN39
-
stRad55A
Sulfolobus tokodaii 7
F9VN39
-
-
SV40 T-antigen
-
-
-
-
triphosphatase
-
-
-
-
V-adenosine triphosphatase
-
-
V-ATPase
-
-
-
-
Walker-type ATPase
Q9V2L3
-
XA21 binding protein 24
-
-
XB24
-
-
XPB1
Q97ZF9
-
-
XPB2
Q97ZV2
-
-
mgatpase
-
-
-
-
additional information
-
Lon belongs to the ATPases associated with a variety of cellular activities AAA+ superfamily possessing conserved Walker A and Walker B motifs
additional information
-
the enzyme is a KaiC homologue and belongs to the RecA ATPase superfamily
additional information
Pyrococcus horikoshii OT-3
-
the enzyme is a KaiC homologue and belongs to the RecA ATPase superfamily
-
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acidianus ambivalens DSM 3772
-
-
-
Manually annotated by BRENDA team
strain KM
-
-
Manually annotated by BRENDA team
Bacillus megaterium KM
strain KM
-
-
Manually annotated by BRENDA team
gene CHD1L
-
-
Manually annotated by BRENDA team
young Swiss strain male albino mice
-
-
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
-
-
Manually annotated by BRENDA team
strain DSM 639
-
-
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
XB24 promotes autophosphorylation of XA21 through its ATPase activity. ATPase activity is essential for XB24-mediated regulation of XA21 function
physiological function
-
role for cell surface F1-adenosine triphosphatase in T cell activation by tumors and specific interactions between Vgamma9Vdelta2 TCRs and purified F1-ATPase. Contact of T cells with F1-ATPase on polystyrene beads can partially replace the cell-cell contact stimulus during phosphoantigen responses
physiological function
Q9V2L3
the enzyme plays an essential role in the initiation of chromosomal DNA replication in archaea
physiological function
F9VN39
the enzyme is involved in the recombination by blocking the assembly of stRadA to ssDNA and mediating the recombinase on stSSB-coated ssDNA. Physical interaction may occur between stSSB and stRad55A in this process
physiological function
Sulfolobus tokodaii 7
-
the enzyme is involved in the recombination by blocking the assembly of stRadA to ssDNA and mediating the recombinase on stSSB-coated ssDNA. Physical interaction may occur between stSSB and stRad55A in this process
-
additional information
-
zoledronate treatment promotes F1-expression as well as endogenous phosphoantigen production. Recognition of phosphoantigens on cell membranes in the form of nucleotide derivatives that can bind to F1-ATPase acting as a presentation molecule
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q04544
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O28983
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q97V06, Q97W25
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
115% of the activity with ATP
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
preferred substrate
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ABCA1 plays a major role in cholesterol homeostasis and high density lipoprotein metabolism. ABCA1 translocates phospholipids and cholesterol directly or indirectly to form pre-beta HDL, mechanism, overview
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
Lon is an ATP-dependent serine protease that degrades damaged and certain regulatory proteins in vivo. Lon exists as a homooligomer and represents one of the simplest ATP-dependent proteases because both the protease and ATPase domains are located within each monomeric subunit, ATP and peptide hydrolysis are not stoichiometrically linked, overview, ATP binding and hydrolysis at both the high- and low-affinity sites are necessary for optimal peptide cleavage and the stabilization of the conformational change associated with nucleotide binding
-
-
ir
ATP + H2O
ADP + phosphate
show the reaction diagram
-
enzymatic hydrolysis of ATP by ATPase is an ubiquitous property of cells which is important for intracellular transfer of energy
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
hydrolyzes the magnesium salts of ATP, GTP, and ITP at approximately the same rate
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme catalyzes efficient D-loop formation and strand exchange at temperatures of 60-70C
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the physiological function of the enzyme is unknown. It has ATP-dependent chaperone activity and can prevent the thermal aggregation of proteins in vitro. The ability to interact with non-native proteins resides in the N-domain and is energy-independent
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
single-stranded DNA-dependent ATPase, catalyzes high temperature D-loop formation, recombinase activity, the enzyme is capable of promoting strand transfer through at least 1200 bp of duplex DNA
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
in the presence of Mn2+, the enzyme shows the highest activity with ATP, while UTP, GTP and CTP are only poor substrates
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
F9VN39
ssDNA-dependent ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q97VZ8
the enzyme functions as an ATPase that binds tightly to single-stranded DNA. ATP hydrolysis is less efficient in the presence of dsDNA and in the absence of DNA. It is not an active recombinase in vitro
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q97ZF9, Q97ZV2
the enzyme has minimal ATPase activity in the absence of DNA, which is stimulated by double-stranded PhiX174 supercoiled plasmid DNA and, to a significantly greater extent, by single-stranded PhiX174 virion DNA. No helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the hydrolytic rates of GTP and ITP are substantially higher than for ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Sulfolobus tokodaii 7
F9VN39
ssDNA-dependent ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Acidianus ambivalens DSM 3772
-
-, the hydrolytic rates of GTP and ITP are substantially higher than for ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
in the presence of Mn2+, the enzyme shows the highest activity with ATP, while UTP, GTP and CTP are only poor substrates
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q97V06, Q97W25
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q97VZ8
the enzyme functions as an ATPase that binds tightly to single-stranded DNA. ATP hydrolysis is less efficient in the presence of dsDNA and in the absence of DNA. It is not an active recombinase in vitro
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Q97ZF9, Q97ZV2
the enzyme has minimal ATPase activity in the absence of DNA, which is stimulated by double-stranded PhiX174 supercoiled plasmid DNA and, to a significantly greater extent, by single-stranded PhiX174 virion DNA. No helicase activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Bacillus megaterium KM
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
hydrolyzes the magnesium salts of ATP, GTP, and ITP at approximately the same rate
-
-
?
ATP + H2O
AMP + diphosphate
show the reaction diagram
-
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
37% of the activity with ATP
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
Q04544
about 35% of activity with ATP
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
58% of the activity with ATP, pH 6.0
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
activity for hydrolysis of CTP is 30% compared to hydrolysis of ATP
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
hydrolyzes the magnesium salts of CTP at 2% the rate compared to ATP
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
-
-
-
?
dATP + H2O
dADP + phosphate
show the reaction diagram
-
-
-
-
?
dCTP + H2O
dCDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
Q04544
about 90% of activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
72% of the rate with ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
77.5% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
91% of the activity with ATP, pH 6.0
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
activity for hydrolysis of GTP is 2.4fold higher compared to hydrolysis of ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
hydrolyzes the magnesium salts of ATP, GTP, and ITP at approximately the same rate
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
Acidianus ambivalens, Acidianus ambivalens DSM 3772
-
depending on pH-value the activity is 30-40% higher than activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
Bacillus megaterium KM
-
72% of the rate with ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
hydrolyzes the magnesium salts of ATP, GTP, and ITP at approximately the same rate
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
73% of the activity with ATP
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
100% of the rate with ATP
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
84% of the activity with ATP, pH 6.0
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
activity for hydrolysis of ITP is 2.2fold higher compared to hydrolysis of ATP
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
hydrolyzes the magnesium salts of ATP, GTP, and ITP at approximately the same rate
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
Acidianus ambivalens, Acidianus ambivalens DSM 3772
-
depending on pH-value the activity is 50-60% higher than activity with ATP
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
Bacillus megaterium KM
-
100% of the rate with ATP
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
31% of the activity with ATP
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
Q04544
about 35% of activity with ATP
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
34% of the activity with ATP, pH 6.0
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
hydrolyzes the magnesium salt of UTP at 20% the rate compared to ATP
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
hydrolyzes the magnesium salts of ATP, GTP, and ITP at approximately the same rate
-
-
?
additional information
?
-
-
enzyme helicase activity, is able to unwind double-stranded DNA or RNA in presence of ATP or dATP and divalent cation
-
-
-
additional information
?
-
-
helicase activity with RNA duplex
-
-
-
additional information
?
-
-
the enzyme catalyzes the unwinding of DNA duplex
-
-
-
additional information
?
-
Q04544
the enzyme does not possess helicase activity
-
-
-
additional information
?
-
-
no substrate: ADP, diphosphate, 4-nitrophenyl phosphate
-
-
-
additional information
?
-
-
no substrate: diphosphate, ADP
-
-
-
additional information
?
-
-
the chromodomain helicase/adenosine triphosphatase DNA binding protein 1-like gene, encoding the enzyme, is a possible oncogene responsible for development of hepatocellular carcinomas by inhibition of apoptosis in the cells, molecular mechanism of CHD1L in hepatocarcinogenesis, overview. Interaction of CHD1L and Nur77 inhibits the nucleus-to-mitochondria translocation of Nur77, a critical member of a p53-independent apoptotic pathway, and the subsequent apoptotic pathway
-
-
-
additional information
?
-
-
V-ATPase-dependent vacuolar acidification
-
-
-
additional information
?
-
-
no activity with UTP, ADP, AMP or 4-nitrophenyl phosphate
-
-
-
additional information
?
-
Acidianus ambivalens, Acidianus ambivalens DSM 3772
-
ADP and pyrophosphate are hydrolyzed with small rates, AMP is not hydrolyzed at all
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
ABCA1 plays a major role in cholesterol homeostasis and high density lipoprotein metabolism. ABCA1 translocates phospholipids and cholesterol directly or indirectly to form pre-beta HDL, mechanism, overview
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
Lon is an ATP-dependent serine protease that degrades damaged and certain regulatory proteins in vivo. Lon exists as a homooligomer and represents one of the simplest ATP-dependent proteases because both the protease and ATPase domains are located within each monomeric subunit, ATP and peptide hydrolysis are not stoichiometrically linked, overview
-
-
ir
ATP + H2O
ADP + phosphate
show the reaction diagram
-
enzymatic hydrolysis of ATP by ATPase is an ubiquitous property of cells which is important for intracellular transfer of energy
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the enzyme catalyzes efficient D-loop formation and strand exchange at temperatures of 60-70C
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
the physiological function of the enzyme is unknown. It has ATP-dependent chaperone activity and can prevent the thermal aggregation of proteins in vitro. The ability to interact with non-native proteins resides in the N-domain and is energy-independent
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Acidianus ambivalens DSM 3772
-
-
-
-
?
additional information
?
-
-
the chromodomain helicase/adenosine triphosphatase DNA binding protein 1-like gene, encoding the enzyme, is a possible oncogene responsible for development of hepatocellular carcinomas by inhibition of apoptosis in the cells, molecular mechanism of CHD1L in hepatocarcinogenesis, overview. Interaction of CHD1L and Nur77 inhibits the nucleus-to-mitochondria translocation of Nur77, a critical member of a p53-independent apoptotic pathway, and the subsequent apoptotic pathway
-
-
-
additional information
?
-
-
V-ATPase-dependent vacuolar acidification
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation, Ca2+ is preferred over Mg2+
Ca2+
-
solubilized enzyme, 359% of initial acitivity in presence of 1 mM. For pH value above 6.5, inhibitory above 2.5 mM
Ca2+
-
for maximal catalytic activity, the membrane-bound enzyme requires divalent cations. The most effective cation is magnesium, followed by the slightly less active manganese and the substantially less active calcium
Ca2+
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
ATPase activity is stimulated; highly active with Ca2+ as divalent cation; highly active with Mn2+ as divalent cation; supports activity
Co2+
Q97V06, Q97W25
Co2+ gives 70% of the activity measured with Mg2+
K+
-
100-300 mM, activation of ATPase reaction to about 200% of control
K+
-
ATPase activity is stimulated by 50 mM K+. Replacing 50 mM KCl with 50 mM choline chloride in the buffer results in a substantial loss of ATPase activity
Mg2+
-
activity is absolutely dependent on Mg2+ or Mn2+, maximal activity at 2.5-10 mM
Mg2+
Q04544
20 mM, about 50% of the maximal activation obtained with Mn2+
Mg2+
-
required. 150% of the control at an optimum Mg2+ concentration of 1-3 mM
Mg2+
-
activation at low concentration, Ca2+ is preferred over Mg2+. Inhibitory above 2 mM
Mg2+
-
divalent cation required
Mg2+
-
or Mn2+, strictly required
Mg2+
-
solubilized enzyme, 245% of initial acitivity in presence of 1 mM, inhibitory above 2.5 mM
Mg2+
-
required
Mg2+
-
absolute requirement for a divalent cation. Mg2+ and Mn2+ are equally effective. ATPase activity increased with the Mg/ATP ratio (ATP = 12.5 mM), reaching a maximum between 0.25 and 0.5
Mg2+
-
no ATP hydrolysis in absence of Mg2+
Mg2+
Q97Y08
associated with the active site of each monomer
Mg2+
Q97V06, Q97W25
most active in the presence of Mg2+ cations
Mg2+
-
for maximal catalytic activity, the membrane-bound enzyme requires divalent cations. The most effective cation is magnesium, followed by the slightly less active manganese and the substantially less active calcium. At pH 5.5 the optimal ATP:Mg2+ ratio is 2:1. At pH 7 the optimal ATP:Mg2+ ratio is 4:1. Inhibition at higher Mg2+ concentrations
Mg2+
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
supports ATPase activity; supports poorly the ATPase activity; supports poorly the ATPase activity; supports poorly the ATPase activity
Mn2+
-
activity is absolutely dependent on Mg2+ or Mn2+, maximal activity at 2.5-10 mM
Mn2+
Q04544
activates, 3.5-5 mM MnCl2 are optimal at an ATP concentration of 0.5 mM
Mn2+
-
divalent cation required. 129% of the activity with Mg2+, pH 6.0
Mn2+
-
or Mg2+, strictly required
Mn2+
-
absolute requirement for a divalent cation. Mg2+ and Mn2+ are equally effective. ATPase activity increased with the Mg/ATP ratio (ATP = 12.5 mM), reaching a maximum between 0.25 and 0.5
Mn2+
Q97V06, Q97W25
Mn2+ ions gives 40% of the activity measured with Mg2+
Mn2+
-
for maximal catalytic activity, the membrane-bound enzyme requires divalent cations. The most effective cation is magnesium, followed by the slightly less active manganese and the substantially less active calcium
Na+
-
100-300 mM, activation of ATPase reaction to about 200% of control
Na+
-
enzyme activity is about 70% in the presence of 50 mM Na+ compared to 50 mM K+
Mn2+
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
highly active with Mn2+ as divalent cation; highly active with Mn2+ as divalent cation; highly active with Mn2+ as divalent cation; highly active with Mn2+ as divalent cation
additional information
-
divalent cation is not absolutely required
additional information
-
Ca2+ may not substitute for Mg2+, Mn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
4-chloro-7-nitrobenzofurazan
-
-
-
5-fluoro-2-selenocytosine
-
IC50: 0.075 mM for NTPase reaction, no influence to helicase activity up to a concentration of 0.5 mM
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
ADP
-
competitive
ADP
-
inhibition of ATPase activity, GTPase activity is insensitive
aflatoxin
-
obtained from growing Aspergillus parasiticus in SMKY liquid medium, inhibits enzyme activity at high doses in vivo in testis, liver and kidney, curcumin along with aflatoxin ameliorates aflatoxin-induced changes in adenosine triphosphatase activities
Ca2+
-
solubilized enzyme, 359% of initial acitivity in presence of 1 mM. For pH value above 6.5, inhibitory above 2.5 mM
CaCl2
Q04544
in presence of Mn2+, 10 mM MgCl2 inhibits 20%
Co2+
-
2.5 mM, 61% residual activity
EDTA
-
0.1 mM, complete loss of activity
etretinate
-
-
HCl
-
0.1 M, irreversible inactivation
K+
-
above 500 mM
KNO3
-
20 mM, 63% inhibition
Mg2+
-
above 10 mM
Mg2+
-
activation at low concentration. Inhibitory above 2 mM
Mg2+
-
solubilized enzyme, 245% of initial acitivity in presence of 1 mM, inhibitory above 2.5 mM
Mg2+
-
for maximal catalytic activity, the membrane-bound enzyme requires divalent cations. The most effective cation is magnesium, followed by the slightly less active manganese and the substantially less active calcium. At pH 5.5 the optimal ATP:Mg2+ ratio is 2:1. At pH 7 the optimal ATP:Mg2+ ratio is 4:1. Inhibition at higher Mg2+ concentrations
MgCl2
Q04544
in presence of Mn2+, 10 mM MgCl2 inhibits 10%
N,N'-dicyclohexylcarbodiimide
-
-
N,N'-dicyclohexylcarbodiimide
-
1 mM, 20% inhibition of ATPase activity at pH 5.5, 4% inhibition of aTPase activity at pH 7.0
N-Ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
maximal inhibition between 1 mM and 500 mM
Na+
-
above 500 mM
NaCl
Q04544
100 mM, inhibits ATP hydrolysis by 30%
Ni2+
-
2.5 mM, 18% residual activity
nitrate
-
50% residual activity at 8 mM
-
nitrate
-
10 mM, 29% inhibition of ATPase activity at pH 5.5, 36% inhibition of ATPase activity at pH 7.0
-
NO3-
-
50% inhibition at 8 mM, maximal inhibition of 87% at 50 mM
O6-benzyl-N7-chloroethylguanine
-
weak inhibition of NTPase activity, enhances helicase activity
O6-benzylguanine
-
weak inhibitor of ATPase and helicase activity
oligo(dA)25
-
above 0.5 mM, inhibits unwinding reaction
-
p-chloromercuribenzenesulfonate
-
-
p-Chloromercuriphenyl sulfonate
-
500 nM at 35% inhibition. Inhibition is reversed by cysteine
p-hydroxymercuribenzoate
-
-
polyA
Q04544
inhibits to a lesser extent than polyC and polyU
polyC
Q04544
1 mg/l, 70% inhibition
polyG
Q04544
inhibits to a lesser extent than polyC and polyU
polyU
Q04544
1 mg/l, 70% inhibition
quercetin
-
0.2 mM, 44% residual activity
retinoic acid
-
-
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
RNA
Q04544
homopolymeric RNA inhibits under otherwise optimal conditions
SDS
-
inactivation of the enzyme at 12% SDS
SO42-
-
50% inhibition at 25 mM
sodium orthovanadate
-
-
sulfate
-
in the presence of 50 mM sulfate, the ATPase activity at pH 5.5 is inhibited by about 33%, whereas at pH 7 the activity is reduced only about 15%
vanadate
-
no inhibitory effect on the ATPase activity at pH 7.0, whereas a remarkable inhibition at high concentrations can be observed for the activity at pH 5.5
Mn2+
-
2.5 mM, 78% residual activity
additional information
-
not inhibitory: N,N'-dicyclohexylcarbodiimide, azide or vanadate
-
additional information
-
partial digestion with trypsin produces four fragments, 170 and 150 kDa and subsequently 125 and 110 kDa, which are recognized by anti-ABCA1 extracellular domain 1 antibody KM3073, and two fragments, 170 and 120 kDa, which are recognized by anti-ABCA1 NBF2 antibody
-
additional information
-
the enzyme is unaffected by phenylarsine oxide
-
additional information
-
ATPase activity is not affected by azide (10 mM), quercetin (200 mM), or vanadate (10 mM). 1,3-Dicyclohexylcarbodiimide (0.100 mM) is not inhibitory when incubated with the enzyme overnight at pH 6 at room temperature 22C
-
additional information
-
no inhibition by N,N'-dicyclohexylcarbodiimide, N-ethylmaleimide, azide or vanadate
-
additional information
P81413
the ATPase activity of the Cdc6/Orc1 protein is completely suppressed by binding to DNA containing the origin recognition box the Cdc6/Orc1 protein changes its conformation on the ORB sequence in the presence of ATP. This conformational change may have an unknown, important function in the initiation process of DNA replication
-
additional information
-
no effect concanamycin A
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4,5-dihydro-8H-6-(N-phenyl)amino-1-(beta-D-ribofuranosyl)imidazo[4,5-e][1,3]diazepine-4,8-dione
-
activates
Calmodulin
-
-
Na2SO3
-
20 mM, 10.5fold stimulation at pH 7.0, 3.3fold stimulation at pH 5.0; 20 mM, 3fold stimulation at pH 5.0
NaCO3
-
20 mM, 6.8fold stimulation at pH 7.0
-
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(dA)
-
1.7-3.3 mM, activation of ATPase activity to 170-180% of control
ssDNA
F9VN39
the ATP hydrolysis activity of stRad55A is weak in the absence of DNA, and drastically stimulated by ssDNA, but not dsDNA
-
ssDNA
Q97ZF9, Q97ZV2
stimulates ATPase activity; stimulates ATPase activity
-
sulfate
-
10 mM, activating with shift of pH optimum from 6.5 to 5.0
sulfite
-
stimulation of solubilized enzyme
sulfite
-
maximal activation between 5 and 10 mM. Concentrations greater than 10 mM sulfite result in a progressive decrease in the extent of activation and eventual inhibition of ATP hydrolysis
sulfite
-
in the presence of 20 mM Na2SO3 the ATPase activity can be stimulated 2.5fold in the pH range from 5.5 to 7.0. At pH-values higher than 8, no stimulation occurs. After addition of the stimulating anion sulfite (20 mM) the ATPase activity at pH 5.5 is no longer inhibited by high magnesium concentrations, whereas the inhibition by progressive increase of the Mg2+-concentration persists at pH 7
triphosphoric acid 1-adenosin-5'-yl ester 3-(3-methylbut-3-enyl) ester
-
an adenylated derivative of isopentenyl diphosphate, can stably bind to F1-ATPase-coated beads and promotes TCR aggregation, lymphokine secretion, and activation of the cytolytic process provided that nucleotide diphosphatase activity is present. It also acts as an allosteric activator of F1-ATPase
-
verapamil
-
ATPase activity is stimulated by verapamil
HCO3-
-
slight inhibition
additional information
-
curcumin along with aflatoxin ameliorates aflatoxin-induced changes in adenosine triphosphatase activities in testis, liver and kidney of mice
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
-
ATP
-
37C
0.0095
-
ATP
-
-
0.6
-
ATP
-
pH 6.6, 86C
0.98
-
ATP
-
pH 7.5, 37C
1.4
-
ATP
-
pH 7.5, 78C
1.6
-
ATP
-
pH 5.2, 60C, in presence of HSO3-
2.5
-
ATP
-
70C, pH 5.5, at the optimal ATP:Mg ratio of 2:1; 70C, pH 7.0, at the optimal ATP:Mg ratio of 4:1
4
-
ATP
-
70C, pH 5.5, at a constant Mg2+-concentration of 5 mM; 70C, pH 7.0, at a constant Mg2+-concentration of 5 mM
0.0066
-
dATP
-
37C
0.071
-
dCTP
-
37C
0.0000000047
-
DNA duplex
-
-
-
0.002
-
GTP
-
37C
additional information
-
additional information
-
pre-steady-state and steady-state kinetics, functional nonequivalency in the ATPase activity of the enzyme that contains high- and low-affinity ATPase sites, which are noninteracting, overview, ATP and peptide hydrolysis are not stoichiometrically linked
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0043
0.0062
ATP
-
pH and temperature not specified in the publication
0.019
-
ATP
-
pH 8.0, catalysis by high-affinity ATP site
0.21
-
ATP
-
37C
1.4
-
ATP
Q04544
-
1.97
-
ATP
-
pH 7.5, 78C
17.2
-
ATP
-
pH 8.0, catalysis by low-affinity ATP site
133
-
ATP
-
pH 7.5, 30C
1.56
-
dATP
-
37C
0.022
-
dCTP
-
37C
0.088
-
GTP
-
37C
additional information
-
additional information
-
at optimum Mg2+ and saturating ATP concentrations 1 pmol of enzyme unwinds 5.5 fmol of DNA duplex per s
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.4
-
ATP
-
pH 7.5, 78C
22040
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.075
-
5-fluoro-2-selenocytosine
-
IC50: 0.075 mM for NTPase reaction, no influence to helicase activity up to a concentration of 0.5 mM
0.025
-
erythrosin B
-
pH 6.0, 70C
0.4
-
N-Ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
-
pH 6.0, 70C
8
-
nitrate
-
pH 6.0, 70C
-
0.17
-
p-hydroxymercuribenzoate
-
pH 6.0, 70C
0.12
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00000034
-
-
-
0.001
-
-
below, purified recombinant mutant K939M/K1952M enzyme
0.0583
-
A3RM17, -
wild-type strain MSR-1
0.0787
-
A3RM17, -
mutant strain NPHB
0.2
-
-
80C, pH not specified in the publication
0.486
-
-
pH 6.0, 70C
0.5
-
-
above, purified recombinant wild-type enzyme
0.566
-
-
pH 7.5, 70C
5.7
-
-
pH 5.2, 60C
160.8
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
presence of sulfate
5.3
-
-
second optimum at pH 8.0
5.5
7
-
when the ATP:Mg2+ ratio is 4:1. At higher Mg2+-concentrations only one pH-maximum at pH 5.5 can be observed. In the presence of 20 mM Na2SO3 the ATPase activity can be stimulated 2.5fold in the pH range from 5.5 to 7.0
5.5
-
-
second optimum at pH 8.0
6.25
-
-
sole optimum in presence of sulfite
6.5
-
-
absence of sulfate
6.5
-
-
in presence of sulfite
6.5
-
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
assay at; assay at; assay at; assay at
6.6
-
-
assay at
7
7.5
-
assay at
7
-
F9VN39
assay at
7.2
7.5
Q04544
ATPase activity
7.2
-
-
pH optimum for ratio Ca2+/ATP of 1, or Mg2+/ATP of 1.25
7.5
-
-
assay at
7.5
-
Q97V06, Q97W25
mutant enzyme lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN
8
-
-
assay at
8
-
-
second optimum at pH 5.5
additional information
-
-
optimum pH for the enzyme activity varies depending on the ratio of ATP to Mg2+ or Ca2+
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
6.7
-
55C, pH 4.0: about 70% of maximal activity, pH 6.7: about 40% of maximal activity
6
7.6
-
pH 6.0: about 80% of maximal activity, pH 7.6: about 60% of maximal activity
6.8
8
Q04544
pH 6.8: about 90% of maximal activity, pH 8.0: about 70% of maximal activity
7
8
Q97V06, Q97W25
pH 7.0: about 80% of maximal activity, pH 8.0: about 55% of maximal activity, mutant enzyme lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
Q04544
-
30
50
Q97ZF9, Q97ZV2
little increase as the temperature is raised from 30C to 50C
37
-
-
assay at
42
50
-
-
50
60
Q97ZF9, Q97ZV2
-
60
-
F9VN39
assay at
60
-
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
assay at; assay at; assay at; assay at
75
-
Q97V06, Q97W25
mutant enzyme lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN, activity is about a third of wild-type rates
80
-
F9VN39
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
70
Q97ZF9, Q97ZV2
30C-50C: little increase as the temperature is raised from 30C to 50C, 70C: about 50% of maximal activity
40
70
Q97ZF9, Q97ZV2
40C: about 55% of maximal activity, 70C: about 80% of maximal activity
50
100
F9VN39
50C: about 50% of maximal activity, 100C: about 70% of maximal activity
50
80
-
50C: about 50% of maximal activity, 80C: about 80% of maximal activity
65
80
Q97V06, Q97W25
65C: about 40% of maximal activity, 80C: about 75% of maximal activity, no activity at room temperature or 37C, no activity beyond 85C. Mutant enzyme lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN
70
95
-
pH 8.0, 70C: about 55% of maximal activity, 95C: about 50% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
from virus-infected Vero cells
Manually annotated by BRENDA team
-
activated by phosphoantigens provided exogenously or produced by tumors and infected cells. Activation requires a contact between Vgamma9Vdelta2 cells and neighboring cells, F1-ATPase is required for the response to inosine diphosphate
Manually annotated by BRENDA team
additional information
Q04544
viral protein is expressed in Escherichia coli cells
Manually annotated by BRENDA team
additional information
-
ubiquitous presence of the V-ATPase
Manually annotated by BRENDA team
additional information
-
three MHC-I-deficient 721.221 cell lines do not express surface F1-ATPase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
at both poles of Pseudomonas aeruginosa; at one pole of Pseudomonas aeruginosa
Manually annotated by BRENDA team
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
enzyme appears mainly membrane bound, with some protein found in the cytoplasmic fraction of stationary-phase cells
Manually annotated by BRENDA team
-
enzyme appears mainly membrane bound, with some protein found in the cytoplasmic fraction of stationary-phase cells
-
Manually annotated by BRENDA team
Q97V06, Q97W25
the recombinant full-length form (expression in Escherichia coli) is recovered from the membrane fraction and the N-terminally deleted form lacking the transmembrane sequence, MBA2DELTAN, from the cytosolic fraction, but part of the latter protein appears to be membrane-associated
Manually annotated by BRENDA team
-
the recombinant full-length form (expression in Escherichia coli) is recovered from the membrane fraction and the N-terminally deleted form lacking the transmembrane sequence, MBA2DELTAN, from the cytosolic fraction, but part of the latter protein appears to be membrane-associated
-
Manually annotated by BRENDA team
-
four proteins are involved in assembly of the V-subcomplex of the V-ATPase in the endoplasmic reticulum requiring the assembly factors VMA21a or VMA21b, overview
Manually annotated by BRENDA team
-
four proteins are involved in assembly of the V-subcomplex of the V-ATPase in the endoplasmic reticulum requiring yeast assembly factor Vma21p, which can recombinantly be replaced by the Arabidopsis thaliana AtVMA21a and b orthologues, overview
Manually annotated by BRENDA team
-
specific isozyme of V-ATPase
Manually annotated by BRENDA team
-
cytoplasmic membrane
Manually annotated by BRENDA team
Q97V06, Q97W25
bound to; the recombinant full-length form (expression in Escherichia coli) is recovered from the membrane fraction and the N-terminally deleted form lacking the transmembrane sequence, MBA2DELTAN, from the cytosolic fraction, but part of the latter protein appears to be membrane-associated
Manually annotated by BRENDA team
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
enzyme appears mainly membrane bound, with some protein found in the cytoplasmic fraction of stationary-phase cells; gives weak signals in the membrane fractions
Manually annotated by BRENDA team
Bacillus megaterium KM
-
cytoplasmic membrane
-
Manually annotated by BRENDA team
-
bound to; enzyme appears mainly membrane bound, with some protein found in the cytoplasmic fraction of stationary-phase cells; gives weak signals in the membrane fractions; the recombinant full-length form (expression in Escherichia coli) is recovered from the membrane fraction and the N-terminally deleted form lacking the transmembrane sequence, MBA2DELTAN, from the cytosolic fraction, but part of the latter protein appears to be membrane-associated
-
Manually annotated by BRENDA team
-
the enzyme is found in the promastigote plasma membrane, but not in the amastigote plasma membrane. Activity of ATPase in plasma membranes is located at the endoplasmic face of the plasma membrane
Manually annotated by BRENDA team
Acidianus ambivalens DSM 3772
-
loosely attached to
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
153900
-
-
recombinant enzyme, dynamic light-scattering
360000
-
-
gel filtration
370000
-
-
gel filtration
430000
-
-
gel filtration
440000
480000
Q97V06, Q97W25
gel filtration
additional information
-
-
molecular weight above 100000 Da, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 60000, SDS-PAGE
?
-
x * 69000, SDS-PAGE
?
-
x * 63000 + x * 48000 + x * 24000, SDS-PAGE
?
Bacillus megaterium KM
-
x * 69000, SDS-PAGE
-
?
-
x * 63000 + x * 48000 + x * 24000, SDS-PAGE
-
dimer
Q97V06, Q97W25
2 * 69200, wild-type enzyme forms a mixture of dimers and higher oligomers in solution. The mutant lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN forms dimers
dimer
-
; 2 * 69200, wild-type enzyme forms a mixture of dimers and higher oligomers in solution. The mutant lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN forms dimers
-
heptamer
-
3 * 69000 + 3 * 54000 + 1 * 28000, most probable subunit stoichiometry, SDS-PAGE
hexamer
-
3 * 65000, alpha subunit, + 3 * 51000, beta subunit, SDS-PAGE
hexamer
-
6 * 28090, SDS-PAGE
hexamer
-
6 * 40000, ultracentrifugation measurements, the protein forms ring-shaped complexes with a diameter of 125 A. It assembles into hexamers over a wide concentration range both in presence and absence of ATP
hexamer
-
the enzyme forms hexameric complexes, the ability to hexamerize is dependent on the integrity of a GYPL motif in its N-terminal
hexamer
Pyrococcus horikoshii OT-3
-
6 * 28090, SDS-PAGE
-
monomer
Q97VZ8
1 * 30414, mass spectrometry, the enzyme is monomeric in solution in the absence of DNA but forms large molecular mass complexes with predominant peaks at approximately 250000 and 600000 Da when incubated with a 34mer oligonucleotide; 1 * 30416, calculated from sequence, the enzyme is monomeric in solution in the absence of DNA but forms large molecular mass complexes with predominant peaks at approximately 250000 and 600000 Da when incubated with a 34mer oligonucleotide
oligomer
-
x * 67000, SDS-PAGE, Lon exists as a homo-oligomer and represents one of the simplest ATP-dependent proteases because both the protease and ATPase domains are located within each monomeric subunit
oligomer
Q97V06, Q97W25
6 * or 7 * 69200, wild-type enzyme forms a mixture of dimers and higher oligomers in solution. The mutant lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN forms dimers; formation of larger oligomers by the full-length protein under certain conditions
oligomer
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6 * or 7 * 69200, wild-type enzyme forms a mixture of dimers and higher oligomers in solution. The mutant lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN forms dimers; formation of larger oligomers by the full-length protein under certain conditions
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monomer
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1 * 30414, mass spectrometry, the enzyme is monomeric in solution in the absence of DNA but forms large molecular mass complexes with predominant peaks at approximately 250000 and 600000 Da when incubated with a 34mer oligonucleotide; 1 * 30416, calculated from sequence, the enzyme is monomeric in solution in the absence of DNA but forms large molecular mass complexes with predominant peaks at approximately 250000 and 600000 Da when incubated with a 34mer oligonucleotide
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additional information
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the enzyme contains a Walker A motif involved in nucleotide binding
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
SSO2387 shows an autophosphorylation activity
phosphoprotein
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SSO2387 shows an autophosphorylation activity
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Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
vapor diffusion method, using 0.2 M magnesium chloride, 0.1 M Bis-Tris, 25% (w/v) PEG-3350, ADP and MgCl2 at pH 5.5 and 4C (isoform HSPA1A), or 0.2 M trimethyl amine n-oxide, 0.1 M Tris, 26% (w/v) PEG monomethyl ether-2000, ADP and MnCl2, at pH 8.5 and 4C (isoform HSPA1L), or 0.2 M ammonium acetate, 0.1M Bis-Tris, 25% (w/v) PEG-3350, ADP and MgCl2, at pH 5.5 and 4C (isoform HSPA2), or 0.2 M calcium chloride, 0.1 M sodium acetate, 20% (w/v) PEG-6000, ADP and MgCl2, at pH 5.0 and 20C (isoform HSPA5), or 0.1M disodium hydrogen phosphate, 0.1 M citric acid, 16% (w/v) PEG-300, ADP and MgCl2, at pH 3.2 and 20C (isoform HSPA6)
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hanging-drop vapour-diffusion method, crystals belong to the orthorhombic space group C2, with unit-cell parameters a = 79.41, b = 48.63, c = 108.77 A, and diffract to beyond 2.6 A resolution; sitting-drop vapour-diffusion method, hanging-drop vapour-diffusion method, Crystals belong to the orthorhombic space group C2, with unit-cell parameters a = 79.41, b = 48.63, c = 108.77 A, and diffract to beyond 2.6 A resolution
Q9V2L3
ATPase PH0284 in complex with ATP, oil-microbatch technique, 0.001 ml of protein solution containing 18.9 mg/ml protein, 200 mM NaCl, and 20 mM Tris-HCl, pH 8.0, is mixed with 0.001 ml of precipitant solution containing 1.5 M ammonium sulfate, 25% v/v glycerol, and 75 mM Tris-HCl, pH 8.5, sealing with a 1:1 mixture of paraffin oil and silicone, 5-6 days at 22C, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
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sitting-drop vapour diffusion at 20C, hanging-drop vapour-diffusion method, high-resolution crystal structure
Q97VZ8
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
slow inactivation
4
-
-
membrane-bound enzyme is stable, solubilized enzyme is inactivated
50
-
-
activity is rapidly lost upon incubation at 50C
50
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Q97ZF9, Q97ZV2
unstable at temperatures above 50C
70
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Q97ZF9, Q97ZV2
stable up to 70 C
86
-
-
stable at
89
-
-
20 min, no loss of activity
95
-
-
Arrhenius plots for both membrane bound ATPase activities are linear up to 95C, reflecting the enormous thermostability of the enzyme
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-19C, 2 days, enzyme loses about 80% of its initial activity
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4C, stable for at least 3 months
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial, solubilization by dialysis or mild alkali treatment
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release from the membrane by washing with 0.003 M Tris-HCl, pH 7.5
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HiTrap chelating column chromatography and Superdex-200 gel filtration
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recombinant wild-type and mutant His-tagged ABCA1s from insect Sf9 cell microsomal membranes by nickel affinity and anion exchange chromatography
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recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange chromatography, adsorption chromatography, ultrafiltration, and gel filtration to homogeneity
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enrichment
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protein can be easily removed from the membrane by mild treatment with zwitterionic detergents
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expressed and purified without any affinity tag by a combination of heat treatment, heparin and gel-filtration column chromatography; XPB2 is expressed with a cleavable N-terminal polyhistidine tag. The XPB2 protein is unstable at temperatures above 50 C, so the tagged protein is purified without a heat step by immobilised metal affinity chromatography followed by chromatography on a heparin column
Q97ZF9, Q97ZV2
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
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overexpressed in Escherichia coli
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cloning of gene CHD1L, previously called ALC1, within the 1q21 amplicon, by hybrid selection using microdissected DNA from chromosome 1q21
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expressed in Escherichia coli BL21(DE3)R3 pRARE cells
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stable expression of ABCA1 in human fibroblasts WI-38 and HEK-293 cell membranes, expression of His-tagged wild-type and mutant ABCA1s in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
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expression analysis of the ATPase gene of wild-type and mutant enzymes
A3RM17, -
expressed in Escherichia coli
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; expression in Escherichia coli
Q9V2L3
expression in Escherichia coli strain BL21(DE3)
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expression in Escherichia coli
Q97VZ8
expression in Escherichia coli; expression in Escherichia coli
Q97ZF9, Q97ZV2
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
heterologous expression in Escherichia coli with a C-terminal His6-tag; heterologuous expression in Escherichia coli with a C-terminal His6-tag. The full-length form is recovered from the membrane fraction and the N-terminally deleted form lacking the transmembrane sequence, MBA2DELTAN, from the cytosolic fraction, but part of the latter protein appears to be membrane-associated
Q97V06, Q97W25
the selenomethionine derivative of the full length SSO1545 is expressed in Escherichia coli with an N-terminal TEV cleavable His-tag
Q97Y08
expression in Escherichia coli
F9VN39
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the protein is induced at 200 J/m2, and the transcription and translation levels are approximately twofold compared to those in the mock. The transcription and translation levels do not increase at the dose of 100 J/m2
F9VN39
the protein is induced at 200 J/m2, and the transcription and translation levels are approximately twofold compared to those in the mock. The transcription and translation levels do not increase at the dose of 100 J/m2
Sulfolobus tokodaii 7
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K192A
Q97ZF9, Q97ZV2
Walker A box mutant form shows no ATPase activity
up
Q7LXU1, Q7LXX6, Q97VE6, Q97W53
is expressed when the cells are grown on rich medium containing tryptone, sucrose and yeast extract; the expression levels of SSO0120 varies depending on the growth phase. It is highly expressed in the stationary phase of arabinose- and maltose-grown cells and exponentially growing tryptone cells
K192A
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Walker A box mutant form shows no ATPase activity
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up
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is expressed when the cells are grown on rich medium containing tryptone, sucrose and yeast extract; the expression levels of SSO0120 varies depending on the growth phase. It is highly expressed in the stationary phase of arabinose- and maltose-grown cells and exponentially growing tryptone cells
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additional information
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construction of enzyme and enzyme assembly factor knockout mutants V-ATPase-deficient phenotype, overview
additional information
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isolation of a mutant exhibiting about 5% of wild-type activity. Mutant strain is unable to grow on nonfermentable carbon sources and unable to sporulate in glucose-limiting media. Fructose is equally efficient in stimulating ATP synthesis in wild-type and mutant, malate-stimulated ATP synthesis is absent in the mutant
K939M/K1952M
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site-directed mutagenesis of Walker A motif residues, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
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a CHD1L ubiquitous expression transgenic mouse model shows spontaneous tumor formation 24.4% of transgenic mice with the formation of heptaocellular carcinoma in four mice, but not in their 39 wild-type littermates, overview. Silencing CHD1L expression by siRNA restores staurosporine-induced apoptosis
additional information
A3RM17, -
construction of a mutant strain NPHB with 35% increased ATPase activity compared to the wild-type strain, mutant strain NPHB shows 69% increased magnetosome content, accumulates 71% less poly-beta-hydroxybutyrate, and consumes 56% more oxygen and 40% more lactate than wild-type strain MSR-1, phenotype, overview
additional information
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construction of a mutant strain NPHB with 35% increased ATPase activity compared to the wild-type strain, mutant strain NPHB shows 69% increased magnetosome content, accumulates 71% less poly-beta-hydroxybutyrate, and consumes 56% more oxygen and 40% more lactate than wild-type strain MSR-1, phenotype, overview
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S154A
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mutant with negligible ATPase activity
additional information
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V-ATPase-deficient phenotype, overview
K96A
Q97ZF9, Q97ZV2
Walker A box mutant form of xpb2 shows no ATPase activity
additional information
Q97V06, Q97W25
generation of mutants lacking the N-terminal transmembrane helix and lacking the lysine of the Walker A motif in D1 (MBA1DELTAN-K108A) or D2 (MBA1DELTAN-K391A). Mutant K108A has only approx. 65% of the activity shown by MBA1DELTAN (mutant enzyme lacking the N-terminal transmembrane helix), whereas K391A has over 80%, indicating that the bulk of the activity is due to the first AAA domain
K96A
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Walker A box mutant form of xpb2 shows no ATPase activity
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additional information
-
generation of mutants lacking the N-terminal transmembrane helix and lacking the lysine of the Walker A motif in D1 (MBA1DELTAN-K108A) or D2 (MBA1DELTAN-K391A). Mutant K108A has only approx. 65% of the activity shown by MBA1DELTAN (mutant enzyme lacking the N-terminal transmembrane helix), whereas K391A has over 80%, indicating that the bulk of the activity is due to the first AAA domain
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Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATPase activity in the crude alkaline extract of the membrane can recombine with the alkali-treated membrane in the presence of Ca2+ or Mg2+. Upon recombination, 10-40% of the activity becomes protected from cold inactivation at 0C. The purified ATPases can also recombine with the membrane in the presence of Ca2+, with Mg2+ being much less effective
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solubilized ATPase binds back to membranes depleted of ATPase, in the presence of 0.01 M Ca2+. It does not bind to undepleted membranes
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reconstitution of purified recombinant enzyme in lipid vesicles consisting of L-alpha-lecitin from soybean, sphingomyelin, synthesized phospholipids, or sterols, in 40 mM Tris-HCl, pH 7.5, 0.1 mM EGTA, overview
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