Information on EC 3.6.1.3 - adenosinetriphosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.3
-
RECOMMENDED NAME
GeneOntology No.
adenosinetriphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
(Ca2+-Mg2+)-ATPase: no phosphorylated intermediate formed
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NIL
-
-
purine metabolism
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain KM
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain MSR-1
UniProt
Manually annotated by BRENDA team
young Swiss strain male albino mice
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O
AMP + diphosphate
show the reaction diagram
-
-
-
-
?
CTP + H2O
CDP + 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
ITP + H2O
IDP + phosphate
show the reaction diagram
UTP + H2O
UDP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
protease La is an ATP-dependent protease, it requires ATP hydrolysis to digest larger, intact proteins, but can cleave small, fluorogenic peptides such as Glu-Ala-Ala-Phe-MNA by only binding, but not hydrolyzing, ATP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
the enzyme requires NaCl for maximal activity but Na2SO4 and (NH4)2SO4 can substitute. Five times more activity than in the presence of NaCl is observed when 1 M (NH4)2SO4 is present
bafilomycin A1
-
0.001 mM, 64% inhibition
Co2+
Co2+ gives 70% of the activity measured with Mg2+
Dicyclohexylcarbodiimide
-
0.3 mM, 59% inhibition
KNO3
-
100 mM, 14% inhibition
N-ethylmaleimide
-
1 mM, 5% inhibition
Na2SO4
-
the enzyme requires NaCl for maximal activity but Na2SO4 and (NH4)2SO4 can substitute. Sodium sulfate (1.5 M) can substitute to an extent for NaCl resulting in 80% of original enzyme activity
Na3VO4
-
0.1 mM, 32% inhibition
NaCl
-
maximal enzyme activity in the presence of 2.5 M NaCl. The enzyme requires NaCl for maximal activity but Na2SO4 and (NH4)2SO4 can substitute
NaN3
-
5 mM, complete inhibition. Azide can bind via the Mg2+-binding sites (whether ATP is in the active site or not) and inactivate the enzyme. It is a mixed non-competitive inhibitor because it binds more readily to the enzyme than the enzyme/substrate complex
oubain
-
15 mM, complete inhibition
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
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
ATP
-
substrate inhibition of wild-type and mutant enzymes, kinetics, overview
Ca2+
-
solubilized enzyme, 359% of initial acitivity in presence of 1 mM. For pH value above 6.5, inhibitory above 2.5 mM
CaCl2
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
MgCl2
in presence of Mn2+, 10 mM MgCl2 inhibits 10%
Mn2+
-
2.5 mM, 78% residual activity
N,N'-dicyclohexylcarbodiimide
N-Ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
-
-
N-ethylmaleimide
Na+
-
above 500 mM
NaCl
100 mM, inhibits ATP hydrolysis by 30%
NaN3
-
the enzyme is non-competitively inhibited
Ni2+
-
2.5 mM, 18% residual activity
nitrate
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
inhibits to a lesser extent than polyC and polyU
polyC
1 mg/l, 70% inhibition
polyG
inhibits to a lesser extent than polyC and polyU
polyU
1 mg/l, 70% inhibition
quercetin
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
homopolymeric RNA inhibits under otherwise optimal conditions
SDS
-
inactivation of the enzyme at 12% SDS
SO42-
-
50% inhibition at 25 mM
Sodium azide
-
-
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
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
disodium carbonate
-
20 mM, 6.8fold stimulation at pH 7.0
dithiothreitol
-
2 mM, 1.9fold activation
HCO3-
-
slight inhibition
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
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
sulfate
-
10 mM, activating with shift of pH optimum from 6.5 to 5.0
sulfite
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
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 4
ATP
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 133
ATP
1.56
dATP
Reovirus sp.
-
37C
0.022
dCTP
Reovirus sp.
-
37C
0.088
GTP
Reovirus sp.
-
37C
additional information
additional information
West Nile virus
-
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 1.4
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.1
NaN3
-
pH 7.8, 37C, in the presence of Na+, K+, and Mg2+
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.025
erythrosin B
Sulfolobus acidocaldarius
-
pH 6.0, 70C
0.4
N-Ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
Sulfolobus acidocaldarius
-
pH 6.0, 70C
8
nitrate
Sulfolobus acidocaldarius
-
pH 6.0, 70C
0.17
p-hydroxymercuribenzoate
Sulfolobus acidocaldarius
-
pH 6.0, 70C
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000034
-
-
0.001
-
below, purified recombinant mutant K939M/K1952M enzyme
0.0583
wild-type strain MSR-1
0.0787
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
8.4
-
pH 7.8, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
7 - 7.5
-
assay at
7.2
-
pH optimum for ratio Ca2+/ATP of 1, or Mg2+/ATP of 1.25
7.2 - 7.5
ATPase activity
additional information
-
optimum pH for the enzyme activity varies depending on the ratio of ATP to Mg2+ or Ca2+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
pH 6.8: about 90% of maximal activity, pH 8.0: about 70% of maximal activity
7 - 8
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
little increase as the temperature is raised from 30C to 50C
37
-
assay at
42 - 50
-
-
75
mutant enzyme lacking the N-terminal transmembrane helix (residues 127), MBA1DELTAN, activity is about a third of wild-type rates
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
30C-50C: little increase as the temperature is raised from 30C to 50C, 70C: about 50% of maximal activity
40 - 70
40C: about 55% of maximal activity, 70C: about 80% of maximal activity
50 - 80
-
50C: about 50% of maximal activity, 80C: about 80% of maximal activity
50 - 100
50C: about 50% of maximal activity, 100C: about 70% of maximal activity
65 - 80
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
COMMENTARY hide
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
specific isozyme of V-ATPase
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
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)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
-
gel filtration
153900
-
recombinant enzyme, dynamic light-scattering
360000
-
gel filtration
370000
-
gel filtration
430000
-
gel filtration
440000 - 480000
gel filtration
additional information
-
molecular weight above 100000 Da, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heptamer
-
3 * 69000 + 3 * 54000 + 1 * 28000, most probable subunit stoichiometry, SDS-PAGE
hexamer
monomer
oligomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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)
-
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
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
-
sitting-drop vapour diffusion at 20C, hanging-drop vapour-diffusion method, high-resolution crystal structure
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-70
-
cold labile
-20 - 25
-
24 h, the enzyme loses over 50% of its activity
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
labile to storage in nitrogen
-
the addition of 30% sorbitol or 20% glycerol is not effective in maintaining activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-19C, 2 days, enzyme loses about 80% of its initial activity
-
4C, stable for at least 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enrichment
-
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
HiTrap chelating column chromatography and Superdex-200 gel filtration
-
partial, solubilization by dialysis or mild alkali treatment
-
protein can be easily removed from the membrane by mild treatment with zwitterionic detergents
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange chromatography, adsorption chromatography, ultrafiltration, and gel filtration to homogeneity
-
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography and gel filtration
-
recombinant wild-type and mutant His-tagged ABCA1s from insect Sf9 cell microsomal membranes by nickel affinity and anion exchange chromatography
-
release from the membrane by washing with 0.003 M Tris-HCl, pH 7.5
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli
cloning of gene CHD1L, previously called ALC1, within the 1q21 amplicon, by hybrid selection using microdissected DNA from chromosome 1q21
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)R3 pRARE cells
-
expression analysis of the ATPase gene of wild-type and mutant enzymes
expression in Escherichia coli
expression in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli; expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta 2 (DE3)
-
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
overexpressed in Escherichia coli
-
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
-
the selenomethionine derivative of the full length SSO1545 is expressed in Escherichia coli with an N-terminal TEV cleavable His-tag
EXPRESSION
ORGANISM
UNIPROT
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G893A
-
site-directed mutagenesis, the mutant shows 63% of wild-type ATPase activity, 80% of wild-type protease activity, and 2.27fold of the activation by beta-casein compared to the wild-type enzyme
G893A/G894A
-
site-directed mutagenesis, the mutant shows 103% of wild-type ATPase activity, 79% of wild-type protease activity, and 0.745fold of the activation by beta-casein compared to the wild-type enzyme
G893A/G894P
-
site-directed mutagenesis, the mutant shows 112% of wild-type ATPase activity, no protease activity, and 0.32fold of the activation by beta-casein compared to the wild-type enzyme
G893P
-
site-directed mutagenesis, the mutant shows 89% of wild-type ATPase activity, no protease activity, and 0.49fold of the activation by beta-casein compared to the wild-type enzyme
G893P/G894A
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site-directed mutagenesis, the mutant shows 71% of wild-type ATPase activity, 8% of wild-type protease activity, and 0.23fold of the activation by beta-casein compared to the wild-type enzyme
G894A
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site-directed mutagenesis, the mutant shows 139% of wild-type ATPase activity, 76% of wild-type protease activity, and 0.49fold of the activation by beta-casein compared to the wild-type enzyme
G894P
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site-directed mutagenesis, the mutant shows 130% of wild-type ATPase activity, 84% of wild-type protease activity, and 0.23fold of the activation by beta-casein compared to the wild-type enzyme
G894S
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site-directed mutagenesis, the mutant shows 140% of wild-type ATPase activity, 47% of wild-type protease activity, and 0.88fold of the activation by beta-casein compared to the wild-type enzyme
K529R
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site-directed mutagenesis, inactive 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
S855A
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site-directed mutagenesis, the mutant shows 78% of wild-type ATPase activity, no protease activity, and 0.35fold of the activation by beta-casein compared to the wild-type enzyme
T880V
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site-directed mutagenesis, the mutant shows 46% of wild-type ATPase activity, 107% of wild-type protease activity, and 3.28fold of the activation by beta-casein compared to the wild-type enzyme
W770A
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site-directed mutagenesis, the mutant shows 98.5% of wild-type ATPase activity, 6.4% of wild-type protease activity, and 0.305fold of the activation by beta-casein compared to the wild-type enzyme
W770P
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site-directed mutagenesis, the mutant shows 123% of wild-type ATPase activity, 55.3% of wild-type protease activity, and 0.64fold of the activation by beta-casein compared to the wild-type enzyme
S154A
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mutant with negligible ATPase activity
K192A
Walker A box mutant form shows no ATPase activity
K96A
Walker A box mutant form of xpb2 shows no ATPase activity
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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
K192A
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Walker A box mutant form shows no ATPase activity
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K96A
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Walker A box mutant form of xpb2 shows no ATPase activity
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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
Renatured/COMMENTARY
ORGANISM
UNIPROT
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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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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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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Show AA Sequence (4399 entries)
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