Information on EC 3.6.3.15 - Na+-transporting two-sector ATPase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
3.6.3.15
-
RECOMMENDED NAME
GeneOntology No.
Na+-transporting two-sector ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Na+/in = ADP + phosphate + Na+/out
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (Na+-transporting)
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. An enzyme found in alkaliphilic bacteria that is similar to EC 3.6.3.14 (H+-transporting two-sector ATPase) where Na+ replaces H+.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a teleost species of the family Blenniidae inhabiting the intertidal zone of the subtropical sea of Japan, collected using several types of nets at Kuchierabu-jima Island, Yakushima-cho, Kagoshima prefecture
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain DSM 7308
-
-
Manually annotated by BRENDA team
a teleost species of the family Blenniidae inhabiting the intertidal zone of the subtropical sea of Japan, collected using several types of nets at Kuchierabu-jima Island, Yakushima-cho, Kagoshima prefecture
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
a teleost species of the family Blenniidae inhabiting the intertidal zone of the subtropical sea of Japan, collected using several types of nets at Kuchierabu-jima Island, Yakushima-cho, Kagoshima prefecture
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
NHE3-deficient mice show defects in acidification of the epididymal fluid and fertility, phenotype, overview
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate
ATP
show the reaction diagram
ADP + phosphate + Na+/out
ATP + H2O + Na+/in
show the reaction diagram
-
-
-
-
r
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + Li+/in
ADP + phosphate + Li+/out
show the reaction diagram
-
coupled to Li+ translocation across the cytoplasmic membrane
-
-
?
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
show the reaction diagram
ATP + H2O + Na+/in + H+/out
ADP + phosphate + Na+/out + H+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Na/+in
ADP + phosphate + Na/+out
show the reaction diagram
-
-
-
-
?
CDP + phosphate + Na+/out
CTP + H2O + Na+/in
show the reaction diagram
-
lower activity compared to ADP
-
-
r
CTP + H2O
CDP + H2O
show the reaction diagram
CTP + H2O + Na+/in
CDP + phosphate + Na+/out
show the reaction diagram
-
CTP is hydrolyzed at 14% compared to hydrolysis of ATP
-
-
?
GDP + phosphate + Na+/out
GTP + H2O + Na+/in
show the reaction diagram
-
lower activity compared to ADP
-
-
r
GTP + H2O
GDP + phosphate
show the reaction diagram
GTP + H2O + Na+/in
GDP + phosphate + Na+/out
show the reaction diagram
-
GTP is hydrolyzed at 64% compared to hydrolysis of ATP
-
-
?
IDP + phosphate + Na+/out
ITP + H2O + Na+/in
show the reaction diagram
-
lower activity compared to ADP
-
-
r
ITP + H2O
?
show the reaction diagram
-
hydrolyzed at 39% of the activity with ATP
-
-
?
ITP + H2O + Na+/in
IDP + phosphate + Na+/out
show the reaction diagram
-
ITP is hydrolyzed at 99% compared to hydrolysis of ATP
-
-
?
UDP + phosphate + Na+/out
UTP + H2O + Na+/in
show the reaction diagram
-
lower activity compared to ADP
-
-
r
UTP + H2O
UDP + H2O
show the reaction diagram
UTP + H2O + Na+/in
UDP + phosphate + Na+/out
show the reaction diagram
-
UTP is hydrolyzed at 31% compared to hydrolysis of ATP
-
-
?
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
Q2EQR4, Q2EQR5, Q2EQR6, Q2EQR7, Q2EQR8, Q2EQR9, Q2EQS0, Q2EQS1, Q2EQS2
the V-type ATPase pumps Na+ ions out of the cell against the sodium ion motive force at the expense of the hydrolysis of ATP. The enzyme complex consists of an integral membrane part V0 that is responsible for the translocation of the Na+ ions and a cytoplasmic, membrane associated part V1 that hydrolyzes ATP, it functions as two coupled molecular motors
-
-
ir
ATP + H2O + Na+/in
ADP + phosphate + Na+/out
show the reaction diagram
ATP + H2O + Na/+in
ADP + phosphate + Na/+out
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
Carbonyl cyanide m-chlorophenylhydrazone
-
-
Cu2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
Ni2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
Zn2+
-
divalent cations are required for activity. Optimal activity is obtained with MgCl2 (5 mM). MnCl2 (72%) is not superior over MgCl2. Zn2+ (5 mM) can replace Mg2+ to some extent (73%), but Ca2+ (5 mM), Ni2+ (5 mM) and Cu2+ (5 mM) are less effective (47%, 36% or 12%)
additional information
-
no stimulation by Rb+ or Cs+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-(N,N-hexamethylene)-amiloride
-
-
5-(N,N-Hexamethylene)amiloride
-
70% inhibition at 0.1 mM, Na+ protects against inactivation
5-(N-ethyl-N-isopropyl)-amiloride
-
-
5-(N-ethyl-N-isopropyl)amiloride
7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole
-
-
ATPgammaS
-
inhibits ATPase activity but not the Na+ binding capacity of the enzyme
azide
Carbonyl cyanide m-chlorophenylhydrazone
-
0.02 mM, pH 9.0, 75% inhibition with no or low levels of NaCl
destruxin B
dienestrol
-
-
diethylstilbestrol
Furosemide
-
-
H+
-
competitively inhibits binding of Na+ to the K-ring of the enzyme, binding structure, overview
Hexestrol
-
-
Li+
-
competitively inhibits binding of Na+ to the K-ring of the enzyme, binding structure, overview
N',N'-dicyclohexylcarbodiimide
-
inhibition can be relieved by Na+
N,N'-dicyclohexyl-carbodiimide
-
half maximal inhibition at 0.1 mM. N,N'-dicyclohexyl-carbodiimide and Na+ compete for binding to subunit c
N,N'-dicyclohexylcarbodiimide
N,N,N',N'-tetracyclohexyl-1,2-phenylenedioxydiacetamide
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i.e. ETH 2120, complete inhibition. Addition of ETH 2120 to the assay during active transport of Na+ immediately stops further Na+ translocation into the lumen of the proteoliposomes
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N-10-benzylamiloride
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N-ethylmaleimide
-
inhibition of ATPase activity
orthovanadate
-
0.3 mM
tetraphenylboron
-
complete inhibition of ATP-dependent Na+ uptake
tributyltin
-
85% inhibition at 0.001 mM
valinomycin
-
-
vanadate
Venturicidin
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inhibition of both ATPase and Na+ translocation activities
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,5-di-tert-butyl-4-hydroxybenzylidenemalononitrile
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i.e.SF 6847. Transport of Na+ is slightly stimulated, indicating that Na+ transport is electrogenic
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ATP
-
ATP-induced stimulation of proximal tubule Na+-ATPase activity is mediated by a protein kinase C-dependent receptor P2Y2 and/or P2Y4 pathway
bafilomycin A1
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stimulates ATP synthesis
Harmaline
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stimulates ATP synthesis
NaHSO3
-
stimulates
sulfite
-
stimulates activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 17.6
ATP
0.06 - 3.5
Li+/in
0.002 - 5
Na+/in
0.4
Na+/out
-
pH 7.5
additional information
additional information
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Na+ binding kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
destruxin B
-
-
0.2
N-ethylmaleimide
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
dienestrol
Pyrococcus furiosus
-
pH 6.0, 100°C
0.36
diethylstilbestrol
Pyrococcus furiosus
-
pH 6.0, 100°C
0.59
Hexestrol
Pyrococcus furiosus
-
pH 6.0, 100°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00024
-
ATPase activity, R573K mutant, pH 8.8, 20 mM NaCl
0.00114
-
ATPase activity, wild type enzyme, pH 8.8, 20 mM NaCl
0.5
-
enzyme from membrane vesicles, at 40°C in 50 mM MOPS buffer (pH 7.5.)
1.1
-
enzyme after 2.2fold purification, at 40°C in 50 mM MOPS buffer (pH 7.5)
5.8
-
pH 6.0, 100°C
6
-
enzyme after 12fold purification, at 40°C in 50 mM MOPS buffer (pH 7.5)
15
-
enzyme after 30fold purification, at 40°C in 50 mM MOPS buffer (pH 7.5)
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
7 - 9
-
in presence of 5 mM Na+
7.5 - 9
-
at 5 mM of Na+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
pH 5.0: about 20% of maximal activity, pH 5.5: about 85% of maximal activity, pH 9.0: abozt 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
NHE2 and NHE3
Manually annotated by BRENDA team
-
NHE2 at lower level
Manually annotated by BRENDA team
-
NHE1, no NHE3
Manually annotated by BRENDA team
-
NHE2 at lower level
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6000
-
NtpA3, NtpB3, NtpD1, 3 * 6000 + 3 * 52000 + 1 * 29000, SDS-PAGE
7164
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
8000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
8255
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
10000
x * 10000, G subunit, SDS-PAGE, x * 11600, about, G subunit, sequence calculation
11409
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
11600
x * 10000, G subunit, SDS-PAGE, x * 11600, about, G subunit, sequence calculation
12000
x * 12000, F subunit, SDS-PAGE, x * 12300, about, F subunit, sequence calculation
12300
x * 12000, F subunit, SDS-PAGE, x * 12300, about, F subunit, sequence calculation
14184
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
14255
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
16036
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
17000
x * 17000, K subunit, SDS-PAGE, x * 17600, about, K subunit, sequence calculation
17600
x * 17000, K subunit, SDS-PAGE, x * 17600, about, K subunit, sequence calculation
19443
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
20763
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
22699
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
22700
x * 26000, E subunit, SDS-PAGE, x * 22700, about, E subunit, sequence calculation
24000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
24300
x * 25500, D subunit, SDS-PAGE, x * 24300, about, D subunit, sequence calculation
25447
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
25500
x * 25500, D subunit, SDS-PAGE, x * 24300, about, D subunit, sequence calculation
26000
x * 26000, E subunit, SDS-PAGE, x * 22700, about, E subunit, sequence calculation
27093
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
29000
-
NtpA3, NtpB3, NtpD1, 3 * 6000 + 3 * 52000 + 1 * 29000, SDS-PAGE
31709
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
37000
x * 37000, C subunit, SDS-PAGE, x * 38400, about, C subunit, sequence calculation
38162
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
38400
x * 37000, C subunit, SDS-PAGE, x * 38400, about, C subunit, sequence calculation
48869
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
50453
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
51139
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
51200
x * 51000, B subunit, SDS-PAGE, x * 51200, about, B subunit, sequence calculation
55667
-
1 * 14184 + 1 * 25447 + 1 * 8255 + 1 * 19443 + 1 * 20763 + 1 * 55667 + 1 * 31709 + 1 * 50453, calculated from sequence of cDNA
60000
-
SDS-PAGE
65000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
65766
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
69000
-
x * 8000 + x * 14000 + x * 15000 + x * 24000 + x * 27000 + x * 38000 + x * 52000 + x * 65000 + x * 69000, SDS-PAGE
72300
x * 72300, I subunit, SDS-PAGE, x * 72300, about, I subunit, sequence calculation
75619
-
x * 14255, NtpF, + x * 75619, NtpI, + x * 16036, NtpK, + x * 22699, NtpE, + x * 38162, NtpC, + x * 11409, NtpG, + x * 65766, NtpA, + x * 51139, NtpB, + x * 27093, NtpD, + x * 7164, NtpH, x * 48869, NtpJ, calculation from nucleotide sequence
100000
240000
-
V0 domain
400000
500000
-
V1 domain
590000
-
gel filtration
670000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
multimer
-
3 * 66000 + 3 * 51000 + 1 * 38000 + 1 * 27000 + 3 * 23000 + 2 (or 3) * 14000 + 4 (or 6) * 11000 + 1 * 76000 + 2 (or 3) * 16000, SDS-PAGE
nonamer
oligomer
-
? * 57000 + ? * 52000 + ? * 35000 + ? * 19000 + ? * 16000 + ? * 4800, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
-
contains the NtpK proteolipid subunit
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
0.005 ml of 2 mg/ml purified K-ring in 20 mM Tris-HCl, pH 7.5, 100 mM LiCl, 10% glycerol, and 0.32 mM n-dodecyl-beta-D-maltoside by sitting drop vapor diffusion method, mixing with 0.005 ml of reservoir solution consisting of 100 mM Tris-HCl, pH 7.5, 4% glycerol, 240 mM potassium citrate, 1.2 mM undecylmaltoside, and 34% PEG 400, at 20°C, in presence or absence of 10 mM NaCl, first appearance after 3 days, maximal size after 3 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
stable for longer periods
50 - 55
-
stable for 5-10 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
without glycerol, the purified enzyme, 1 mg/ml in 50 mM Tris-HCl, pH 7.5 is inactivated by overnight exposure to 4°C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, solubilized enzyme is stable for at least 3 months
-
-80°C, 10 mM Tris-HCl pH 8.0 containing 2 mM MgCl2 to a protein concentration of 1.5 mg/ml, stable for at least 2 months
-
4°C, 50 mM MOPS pH 7.5, 4 days, no activity loss of the native enzyme
-
4°C, 50 mM MOPS pH 7.5, 5 days, 75% activity loss of the purified enzyme
-
4°C, solubilized enzyme is stable for at least 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration
-
precipitation using polyethylene glycol 6000
-
purification of a His-tagged enzyme by affinity column chromatography
-
purification of the V-ATPase and isolation of the K-ring by by anion exchange chromatography and gel filtration
-
separate purification of His-tagged NtpE and NtpF, and His-tagged N-terminal hydrophilic domain of NtpI by nickel affinity and ion exchange chromatography, and gel filtration
-
using anion-exchange and gel filtration chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of NHE1 from epididymis
-
expressed in Escherichia coli strain DH10B
-
expressed in Oryza sativa cultivar Nipponbare
genes ntpE and ntpF encoding the two subunits of the enzyme, expression of both subunits and the N-terminal soluble domain of NtpI as His-tagged proteins in Escherichia coli strain BL21(DE3)
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ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha; ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha; ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha; ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha; ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha; ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha; ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha; ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha; ntp operon, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the activity of Na+-ATPase is increased in rats receiving weekly hydrodynamic injection (1 mg/kg) of a naked plasmid containing human HGF gene associated with a cytomegalovirus promoter during 6 weeks
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R573E
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inactive mutant
R573K
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mutant can grow in alcaline medium
R573L
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inactive mutant
R573Q
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inactive mutant
additional information
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mutant with a lesion in membrane Na+-translocation is neither inhibited by dicyclohexylcarbodiimide nor stimulated by Na+
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