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ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
2,4-dinitrophenyl phosphate + H2O + Ca2+/in
?
-
-
-
-
?
acyl-carrier protein + H2O + Ca2+/in
?
-
-
-
-
?
ADP + phosphate + Ca2+/in
ATP + H2O + Ca2+/out
-
-
-
r
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O + 2 Ca2+[cytoplasm side]
ADP + phosphate + 2 Ca2+[lumen side]
-
-
-
-
?
ATP + H2O + 2 Ca2+[side 1]
ADP + phosphate + 2 Ca2+[side 2]
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
the enzyme has a much lower affinity for Mn2+ than for Ca2+
-
-
?
ATP + H2O + Sr2+/in
ADP + phosphate + Sr2+/out
-
-
-
?
ATP + Sr2+/cis + H2O
ADP + phosphate + Sr2+/trans
-
-
-
-
?
GTP + H2O + Ca2+/in
GDP + phosphate + Ca2+/out
-
-
-
?
p-nitrophenyl phosphate + H2O + Ca2+/in
?
-
-
-
-
?
UTP + H2O + Ca2+/in
UDP + phosphate + Ca2+/out
-
-
-
?
additional information
?
-
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + 2 Ca2+[side 1]
ADP + phosphate + 2 Ca2+[side 2]
-
-
-
-
?
ATP + H2O + 2 Ca2+[side 1]
ADP + phosphate + 2 Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is the Ca2+ pump in sarcoplasmic reticulum membranes
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is the Ca2+ pump in sarcoplasmic reticulum membranes, the ATP hydrolysis energy is used for uphill transport and accumulation of Ca2+
-
-
r
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
assay with labeled ATP substrate
-
-
r
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
Ca2+ transport
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the enzyme performs ATP-dependent Ca2+/H+ antiport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
sarcoplasmic reticulum Ca-ATPase transports calcium ions from the myoplasm to the reticulum lumen at the expense of ATP hydrolysis
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme has one high affinity ATP binding site (catalytic site) and two calcium-binding sites
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
r
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
-
-
?
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
-
existence of two different conformations of chemically equivalent Ca2+-ATPase: E1, the high affinity state for Ca2+ and E2, the low affinity state for Ca2+
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
additional information
?
-
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
-
-
?
additional information
?
-
-
the ATP-binding cleft is mainly located within the p29/30 domain with the phosphorylation site strategically located at the N-terminal border of this domain
-
-
?
additional information
?
-
interaction of Ca2+-ATPase with phospholamban is involved in regulation of heart contractility, overview
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
additional information
?
-
interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity, the detergent-solubilized enzyme shows monomeric catalytic function as deduced from kinetic modelling, while the native enzyme shows features of oligomeric protein conformational interactions that constrain the subunits to a staggered or out-of-phase mode of action
-
-
?
additional information
?
-
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
additional information
?
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
additional information
?
-
the SERCA 1 Ca2+-ATPase in white muscle is able to work as ion pumps, but clearly also as heat pumps because of their large ATPase activity. This may explain why SERCA 1 type Ca2+-ATPases dominate in tissues where thermal regulation is important.
-
-
?
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(4-chlorophenyl)(pyridin-2-yl)[4-(pyrrolidin-1-ylmethyl)phenyl]methanol
-
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
-
(N-((3-chlorophenyl)(4-(pyrrolidin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
NF1058, inhibits the enzyme SERCA1 stabilizing an E2 state that can still be phosphorylated with phosphate
1,1'-methanediyldinaphthalen-2-ol
-
1,2-dichlorobenzene
-
at concentrations of 0.25-0.75 mM, 1,2-dichlorobenzene inhibits the ATP hydrolysis to about 80%. Starting at 0.05 mM, 1,2-dichlorobenzene is able to uncouple the ratio of hydrolysis/Ca2+transporte
1,3-dibromo-2,4,6-tri(methylisothiouronium)benzene
micromolar inhibitor of SERCA
1-(naphthalen-1-ylmethyl)naphthalen-2-ol
-
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-1,2,4-triazole
-
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-imidazole
-
2,2',2''-methanetriyltris(4-tert-butylphenol)
-
2,2'-methanediylbis(4-tert-butylphenol)
-
2,4-di-tert-butyl-6-(1-phenylethyl)phenol
-
2,4-di-tert-butyl-6-[1-(4-methoxyphenyl)ethyl]phenol
-
2,5-bis(2-methylpropyl)phenol
-
2,5-bis(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol
-
2,5-di(tert-butyl)hydroquinone
micromolar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
2,5-di-tert-butyl-1,4-dihydroxybenzene
stabilizes the enzyme structure in absence of Ca2+, binding site structure and binding mode involving Asp59 and Pro308, overview
2,5-di-tert-butylhydroquinone
-
2,6-di-tert-butyl-4-[1-(4-methoxyphenyl)ethyl]phenol
-
2-(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol
-
2-cyclooctylbenzene-1,4-diol
-
3-(1,1-diphenylethyl)cyclopentanol
-
4,4'-butane-2,2-diylbis(2-methylphenol)
-
4,4'-butane-2,3-diyldiphenol
-
4,4'-propane-2,2-diylbis(2,6-dimethylphenol)
-
4,5-dibenzylbenzene-1,2-diol
-
4-(7-methyloctyl)phenol
-
6-tert-butyl-2,3-dihydro-1H-inden-5-ol
-
7-chloro-4-(piperazin-1-yl)quinoline
-
bis(maltolato)oxovanadium(IV)
-
-
bis(N-hydroxylamidoiminodiacetato)vanadium(IV)
-
-
bupivacaine
-
inhibition by bupivacaine is not competitive with respect to the specific transport and catalytic sites of the enzyme
Ca2+
-
above 0.1 mM, Ca2+-dependent ATPase
detergent C12E8
-
inhibition of mutant D813A/D818A
lidocaine
-
inhibition by lidocaine is not competitive with respect to the specific transport and catalytic sites of the enzyme
N,N-dimethylalkylamine N-oxide
-
slight stimulation at low concentrations, inhibition at higher concentrations, maximal inhibition for the homologue with the alkyl chain length n=16
N-((3-chlorophenyl)(4-((4-(7-chloroquinolin-4-yl)piperazin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
NF1442
N-alkyl-N,N-dimethylamine-N-oxide
-
CnNO with n = 10-20, stimulate at low concentrations and inhibit at high concentrations dependent on the compound alkyl chain length, overview, inhibition occurs due to compound-induced lipid bilayer structure perturbation in the ATPase annular region
palytoxin
-
the inhibition process exhibits the following characteristics: the degree of inhibition is dependent on membrane protein concentration, no protection is observed when the ATP concentration is raised, dependence on Ca2+ concentration with a decreased maximum catalytic rate, and it occurrs in the absence of Ca2+ ionophoric activity
polysubstituted fullerene C60-II
-
noncompetitive and reversible inhibition, complete inhibition at 0.05 mM
-
polysubstituted fullerene C60-III
-
complete inhibition at 0.05 mM
-
polysubstituted fullerene C60-IV
-
76% inhibition of Ca2+ transport and 91% inhibition of ATP hydrolysis at 0.05 mM
-
polysubstituted fullerene C60-IX
-
complete inhibition at 0.05 mM
-
polysubstituted fullerene C60-V
-
complete inhibition at 0.05 mM
-
polysubstituted fullerene C60-VI
-
63% inhibition of Ca2+ transport and 38% inhibition of ATP hydrolysis at 0.05 mM
-
polysubstituted fullerene C60-VII
-
60% inhibition of Ca2+ transport and 38% inhibition of ATP hydrolysis at 0.05 mM
-
polysubstituted fullerene C60-VIII
-
82% inhibition of Ca2+ transport and 67% inhibition of ATP hydrolysis at 0.05 mM
-
polysubstituted fullerene C60-X
-
complete inhibition at 0.05 mM
-
polysubstituted fullerene C60-XI
-
complete inhibition at 0.05 mM
-
pyridine-2,6-dicarboxylatodioxovanadium
-
-
rutin 4'''-O-arachidonate
-
rutin 4'''-O-linolenate
-
[(dihydroindenyl)oxy]acetic acid
-
DIOA
cyclopiazonic acid
-
cyclopiazonic acid
nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
Mg2+
-
required, best at 0.09 mM in all muscle tissue, higher concentration are inhibitory
Mg2+
-
Mg2+ at high concentration (10 mM) and high pH inhibits the ATPase by binding to low affinity sites made available by the high pH in the medium
phospholamban
-
-
phospholamban
phospholamban inhibits the enzyme by reducing the Ca2+ affinity, phospholamban mutant I40A is highly inhibitory, increases the dissociation constant of the enzyme for Ca2+
-
thapsigargin
-
thapsigargin
-
complete inhibition at 0.001 mM
thapsigargin
-
inhibits Ca2+ uptake in musles
thapsigargin
stabilizes the enzyme structure in absence of Ca2+
thapsigargin
nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
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0.152
(4-chlorophenyl)(pyridin-2-yl)[4-(pyrrolidin-1-ylmethyl)phenyl]methanol
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.022 - 0.029
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
0.0013
(N-((3-chlorophenyl)(4-(pyrrolidin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.015
1,1'-methanediyldinaphthalen-2-ol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0273
1-(naphthalen-1-ylmethyl)naphthalen-2-ol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.032
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-1,2,4-triazole
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.057
1-[(4-chlorophenyl)(phenyl)[4-(pyrrolidin-1-ylmethyl)phenyl]methyl]-1H-imidazole
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.0213
2,2',2''-methanetriyltris(4-tert-butylphenol)
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0118
2,2'-methanediylbis(4-tert-butylphenol)
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0338
2,4-di-tert-butyl-6-(1-phenylethyl)phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0353
2,4-di-tert-butyl-6-[1-(4-methoxyphenyl)ethyl]phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0188
2,5-bis(2-methylpropyl)phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0094
2,5-bis(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0454
2,6-di-tert-butyl-4-[1-(4-methoxyphenyl)ethyl]phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0202
2-(cyclopenta-2,4-dien-1-ylmethyl)benzene-1,4-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0115
2-cyclooctylbenzene-1,4-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0497
3-(1,1-diphenylethyl)cyclopentanol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0393
4,4'-butane-2,2-diylbis(2-methylphenol)
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0283
4,4'-butane-2,3-diyldiphenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0195
4,4'-propane-2,2-diylbis(2,6-dimethylphenol)
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0238
4,5-dibenzylbenzene-1,2-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0172
4-(7-methyloctyl)phenol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.0281
6-tert-butyl-2,3-dihydro-1H-inden-5-ol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.00229
biphenyl-2,5-diol
Oryctolagus cuniculus
In 0.1 M KCl, 5 mM MgCl2, 0.5 mM EGTA, 0.004.5 mM calcimycin, 0.7 mM CaCl2, and 20 mM Trizma (pH 7.5)
0.04
bis(maltolato)oxovanadium(IV)
Oryctolagus cuniculus
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C
0.325
bis(N-hydroxylamidoiminodiacetato)vanadium(IV)
Oryctolagus cuniculus
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C
35
clotrimazole
Oryctolagus cuniculus
IC50 about 0.035 mM, in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.0008
N-((3-chlorophenyl)(4-((4-(7-chloroquinolin-4-yl)piperazin-1-yl)methyl)phenyl)methyl)-7-chloro-4-aminoquinoline
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.0004
palytoxin
Oryctolagus cuniculus
-
in 20 mM MOPS, pH 7.0, 80 mM KC1, 5 mM MgCl2, 0.5 mM EGTA, 0.55 mM CaC12, at 25°C
0.025
pyridine-2,6-dicarboxylatodioxovanadium
Oryctolagus cuniculus
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C
0.023
rutin 4'''-O-arachidonate
Oryctolagus cuniculus
at 37°C and pH 7.4
0.05
rutin 4'''-O-erucate
Oryctolagus cuniculus
at 37°C and pH 7.4
0.025
rutin 4'''-O-linoleate
Oryctolagus cuniculus
at 37°C and pH 7.4
0.062
rutin 4'''-O-linolenate
Oryctolagus cuniculus
at 37°C and pH 7.4
0.05
rutin 4'''-O-oleate
Oryctolagus cuniculus
at 37°C and pH 7.4
0.035
rutin 4'''-O-stearate
Oryctolagus cuniculus
at 37°C and pH 7.4
0.064
rutin palmitate
Oryctolagus cuniculus
at 37°C and pH 7.4
0.08
vanadate
Oryctolagus cuniculus
-
in 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl2, 0.05 mM CaCl2, at 25°C
0.127
[(dihydroindenyl)oxy]acetic acid
Oryctolagus cuniculus
-
-
0.022
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
0.029
(4-chlorophenyl)[4-([[3-(4-[3-[(7-chloroquinolin-4-yl)amino]propyl]piperazin-1-yl)propyl]amino]methyl)phenyl]methanone
Oryctolagus cuniculus
in 20 mM MOPS, pH 6.8, 80 mM KCl, 3 mM MgCl2, 0.002 mM A23187, 5 mM sodium azide, and 2 mM EGTA, or 0.2 mM EGTA plus 0.2 mM CaCl2, at 37°C
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D203R
the mutant shows an about 5fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
D203R/R678D
the mutant shows an about 3.5fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
D813A/D818A
-
the mutant displays a very low activity in presence of detergent, but the same maximal velocity and apparent affinity for Ca2+ as the wild-type enzyme in absence of detergent, the mutation affects pronotation-dependent winding and unwinding events in the nearby M6 transmembrane segment
E243G/Q244G
-
the mutant shows wild type-like Ca2+-ATPase activity
E439A
the mutant shows an about 15fold basal dephosphorylation rate constant compared to the wild type enzyme
E439S
the mutant shows an about 10fold basal dephosphorylation rate constant compared to the wild type enzyme
E90A
the mutant shows a reduction of the apparent affinity for luminal Ca2+ and exhibits 19% of wild type activity
E90L
the mutant shows a reduction of the apparent affinity for luminal Ca2+ and exhibits less than 10% of wild type activity
E90R
the mutation allows E2P formation from phosphate even at luminal Ca2+ concentrations much too small to support phosphorylation in wild type. The mutant with less than 10% of wild type activity further displays a blocked dephosphorylation of E2P and an increased rate of conversion of the ADP-sensitive E1P phosphoenzyme intermediate to ADP-insensitive E2P as well as insensitivity of the E2-BeF3-complex to luminal Ca2+
I188A
-
displays about 30% reduced ATP turnover rate relative to wild type, whereas the ATP turnover rate is reduced by about 80%
I188F
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is slightly lower (by less than 15%) than that of wild type enzyme, the mutant displays reduced MgATP affinity
K204A
-
the mutant displays around 40% Ca2+ transport, compared with its about 70% rate of ATP turnover relative to the wild type enzyme
K205A
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP slightly lower than that of wild type enzyme
K205E
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is slightly lower (by less than 15%) than that of wild type enzyme, the mutant displays reduced MgATP affinity
K234A
-
the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
K234G
-
the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
K297A
the mutant exhibits 87% of wild type activity
N34A
loss-of-function mutation
Q202A
th mutation causes reduced Ca2+ transport and ATPase activity
Q202A/D203A
the mutant shows an about 4fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
R174A
-
the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP is similar to, or slightly lower than (by less than 15%) that of wild type enzyme, the mutant displays wild type-like MgATP affinity
R174E
-
the mutant displays wild type-like MgATP affinity
R678A
the mutant shows a reduced basal dephosphorylation rate constant compared to the wild type enzyme
R678D
the mutant shows an about 6fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
R678Q
the mutant shows an about 1.4fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
S186A
the mutant shows an about 6fold increased basal dephosphorylation rate constant compared to the wild type enzyme
S186E
the mutant shows an about 1,2fold reduced basal dephosphorylation rate constant compared to the wild type enzyme
S186E/E439S
the mutant restores the basal dephosphorylation rate to a level about 2fold faster than that of the wild type. Little stimulation of the dephosphorylation by ATPis seen in this mutant
S186P
the mutant shows an about 18fold increased basal dephosphorylation rate constant compared to the wild type enzyme
S72A
the mutant exhibits 80% of wild type activity
S72R
the mutation allows E2P formation from phosphate even at luminal Ca2+ concentrations much too small to support phosphorylation in wild type. The mutant with less than 10% of wild type activity further displays a blocked dephosphorylation of E2P and an increased rate of conversion of the ADP-sensitive E1P phosphoenzyme intermediate to ADP-insensitive E2P as well as insensitivity of the E2-BeF3-complex to luminal Ca2+
S766C
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
S766L
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
S766V
the mutation of isoform SERCA1a strongly reduces the apparent Ca2+ affinity and ATPase activity of the enzyme
additional information
-
the deletion of either Glu243 or Gln244 results in a decrease in the relative Ca2+-ATPase activity, 1G and 3G inserts at site 2 have severe consequences consistent with the lack of measurable Ca2+ transport
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Hasselbach, W.
Calcium-activated ATPase of the sarcoplasmic reticulum membranes
New Compr. Biochem.
2
183-208
1981
Oryctolagus cuniculus
-
brenda
Taylor, K.A.; Dux, L.; Varga, S.; Ting-Beall, H.P.; Martonosi, A.
Analysis of two-dimensional crystals of Ca2+-ATPase in sarcoplasmic reticulum
Methods Enzymol.
157
271-289
1988
Oryctolagus cuniculus
brenda
Hasselbach, W.
The reversibility of the sarcoplasmic calcium pump
Biochim. Biophys. Acta
515
23-53
1978
Oryctolagus cuniculus
brenda
Nakamura, J.
Two types of proton-modulated calcium binding in the sarcoplasmic reticulum Ca2+-ATPase. II. Characterization of their calcium bindings
J. Biol. Chem.
269
30822-30827
1994
Oryctolagus cuniculus
brenda
Fassold, E.; Hasselbach, W.
Synthesis of ATP from Ca2+ gradient by sarcoplasmic reticulum Ca2+ transport ATPase
Methods Enzymol.
157
220-228
1988
Oryctolagus cuniculus
brenda
Zarain-Herzberg, A.; MacLennan, D.H.; Pariasamy, M.
Characterization of rabbit cardiac sarco(endo)plasmic reticulum Ca2+-ATPase gene
J. Biol. Chem.
265
4670-4677
1990
Oryctolagus cuniculus
brenda
Michelangeli, F.; Munkonge, F.M.
Methods of reconstitution of the purified sarcoplasmic reticulum (Ca2+-Mg2+)-ATPase using bile salt detergents to form membranes of defined lipid to protein ratios or sealed vesicles
Anal. Biochem.
194
231-236
1991
Oryctolagus cuniculus
brenda
Andriamainty, F.; Filipek, J.; Devinsky, F.; Balgavy, P.
Effects of N,N-dimethylalkylamine N-oxides on the activity of purified sarcoplasmic reticulum (Ca-Mg)ATPase
Pharmazie
52
240-242
1997
Oryctolagus cuniculus
brenda
Champeil, P.; Menguy, T.; Soulie, S.; Juul, B.; Gomez de Garcia, A.; Rusconi, F.; Falson, P.; Denoroy, L.; Henao, F.; le Maire, M.; Moeller, J.V.
Characterization of a protease-resistant domain of the cytosolic portion of sarcoplasmic reticulum Ca2+-ATPase
J. Biol. Chem.
273
6619-6631
1998
Oryctolagus cuniculus
brenda
Chen, B.; Squier, T.C.; Bigelow, D.J.
Calcium activation of the Ca-ATPase enhances conformational heterogeneity between nucleotide binding and phosphorylation domains
Biochemistry
43
4366-4374
2004
Oryctolagus cuniculus
brenda
Dode, L.; Vilsen, B.; Van Baelen, K.; Wuytack, F.; Clausen, J.D.; Andersen, J.P.
Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 3 isoforms by steady-state and transient kinetic analyses
J. Biol. Chem.
277
45579-45591
2002
Oryctolagus cuniculus, Homo sapiens
brenda
Lenoir, G.; Picard, M.; Moller, J.V.; le Maire, M.; Champeil, P.; Falson, P.
Involvement of the L6-7 loop in SERCA1a Ca2+-ATPase activation by Ca2+ (or Sr2+) and ATP
J. Biol. Chem.
279
32125-32133
2004
Oryctolagus cuniculus
brenda
Toyoshima, C.; Mizutani, T.
Crystal structure of the calcium pump with a bound ATP analogue
Nature
430
529-535
2004
Oryctolagus cuniculus (P04191)
brenda
Mahaney, J.E.; Thomas, D.D.; Froehlich, J.P.
The time-dependent distribution of phosphorylated intermediates in native sarcoplasmic reticulum Ca2+-ATPase from skeletal muscle is not compatible with a linear kinetic model
Biochemistry
43
4400-4416
2004
Oryctolagus cuniculus
brenda
Peinelt, C.; Apell, H.J.
Kinetics of Ca2+ binding to the SR Ca-ATPase in the E1 state
Biophys. J.
89
2427-2433
2005
Oryctolagus cuniculus
brenda
Stokes, D.L.; Pomfret, A.J.; Rice, W.J.; Glaves, J.P.; Young, H.S.
Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals
Biophys. J.
90
4213-4223
2006
Oryctolagus cuniculus (P04191)
brenda
Sorensen, T.L.; Olesen, C.; Jensen, A.M.; Moller, J.V.; Nissen, P.
Crystals of sarcoplasmic reticulum Ca2+-ATPase
J. Biotechnol.
124
704-716
2006
Oryctolagus cuniculus (P04191)
brenda
Sanchez, G.A.; Takara, D.; Toma, A.F.; Alonso, G.L.
Characteristics of the sarcoplasmic reticulum Ca2+-dependent ATPase from masticatory muscles
J. Dent. Res.
83
557-561
2004
Oryctolagus cuniculus
brenda
Karlovska, J.; Hammel, M.; Laggner, P.; Lacko, I.; Devinsky, F.; Balgavy, P.
Effects of N-alkyl-N,N-dimethylamine-N-oxides on the activity of purified sarcoplasmic reticulum Ca(2+)-transporting ATPase
Pharmazie
60
135-137
2005
Oryctolagus cuniculus
brenda
Jidenko, M.; Nielsen, R.C.; S?rensen, T.L.; M?ller, J.V.; le Maire, M.; Nissen, P.; Jaxel, C.
Crystallization of a mammalian membrane protein overexpressed in Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
102
11687-11691
2005
Oryctolagus cuniculus (P04191), Oryctolagus cuniculus
brenda
Obara, K.; Miyashita, N.; Xu, C.; Toyoshima, I.; Sugita, Y.; Inesi, G.; Toyoshima, C.
Structural role of countertransport revealed in Ca2+ pump crystal structure in the absence of Ca2+
Proc. Natl. Acad. Sci. USA
102
14489-14496
2005
Gallus gallus, Oryctolagus cuniculus (P04191)
brenda
Jidenko, M.; Lenoir, G.; Fuentes, J.M.; le Maire, M.; Jaxel, C.
Expression in yeast and purification of a membrane protein, SERCA1a, using a biotinylated acceptor domain
Protein Expr. Purif.
48
32-42
2006
Oryctolagus cuniculus
brenda
Fujii, T.; Ohira, Y.; Itomi, Y.; Takahashi, Y.; Asano, S.; Morii, M.; Takeguchi, N.; Sakai, H.
Inhibition of P-type ATPases by [(dihydroindenyl)oxy]acetic acid (DIOA), a K+ -Cl- cotransporter inhibitor
Eur. J. Pharmacol.
560
123-126
2007
Oryctolagus cuniculus
brenda
Toyoshima, C.
Structural aspects of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum
Arch. Biochem. Biophys.
476
3-11
2008
Oryctolagus cuniculus (P04191)
brenda
Zafar, S.; Hussain, A.; Liu, Y.; Lewis, D.; Inesi, G.
Specificity of ligand binding to transport sites: Ca2+ binding to the Ca2+ transport ATPase and its dependence on H+ and Mg2+
Arch. Biochem. Biophys.
476
87-94
2008
Oryctolagus cuniculus
brenda
Coca, R.; Soler, F.; Fernandez-Belda, F.
Characterization of the palytoxin effect on Ca2+-ATPase from sarcoplasmic reticulum (SERCA)
Arch. Biochem. Biophys.
478
36-42
2008
Oryctolagus cuniculus
brenda
Afara, M.R.; Trieber, C.A.; Ceholski, D.K.; Young, H.S.
Peptide inhibitors use two related mechanisms to alter the apparent calcium affinity of the sarcoplasmic reticulum calcium pump
Biochemistry
47
9522-9530
2008
Oryctolagus cuniculus (P04191)
brenda
Deye, J.; Elam, C.; Lape, M.; Ratliff, R.; Evans, K.; Paula, S.
Structure-based virtual screening for novel inhibitors of the sarco/endoplasmic reticulum calcium ATPase and their experimental evaluation
Bioorg. Med. Chem.
17
1353-1360
2009
Oryctolagus cuniculus (P04191)
brenda
Arruda, A.P.; Ketzer, L.A.; Nigro, M.; Galina, A.; Carvalho, D.P.; de Meis, L.
Cold tolerance in hypothyroid rabbits: role of skeletal muscle mitochondria and sarcoplasmic reticulum Ca2+ ATPase isoform 1 heat production
Endocrinology
149
6262-6271
2008
Oryctolagus cuniculus (P04191), Oryctolagus cuniculus
brenda
Kjelstrup, S.; de Meis, L.; Bedeaux, D.; Simon, J.M.
Is the Ca2+-ATPase from sarcoplasmic reticulum also a heat pump?
Eur. Biophys. J.
38
59-67
2008
Oryctolagus cuniculus, Oryctolagus cuniculus (P04191), Oryctolagus cuniculus (P20647)
brenda
Aureliano, M.; Henao, F.; Tiago, T.; Duarte, R.O.; Moura, J.J.; Baruah, B.; Crans, D.C.
Sarcoplasmic reticulum calcium ATPase is inhibited by organic vanadium coordination compounds: pyridine-2,6-dicarboxylatodioxovanadium(V), BMOV, and an amavadine analogue
Inorg. Chem.
47
5677-5684
2008
Oryctolagus cuniculus
brenda
Clausen, J.D.; McIntosh, D.B.; Woolley, D.G.; Andersen, J.P.
Critical interaction of actuator domain residues arginine 174, isoleucine 188, and lysine 205 with modulatory nucleotide in sarcoplasmic reticulum Ca2+-ATPase
J. Biol. Chem.
283
35703-35714
2008
Oryctolagus cuniculus
brenda
Holdensen, A.N.; Andersen, J.P.
The length of the A-M3 linker is a crucial determinant of the rate of the Ca2+ transport cycle of sarcoplasmic reticulum Ca2+-ATPase
J. Biol. Chem.
284
12258-12265
2009
Oryctolagus cuniculus
brenda
Mangialavori, I.; Giraldo, A.M.; Buslje, C.M.; Gomes, M.F.; Caride, A.J.; Rossi, J.P.
A new conformation in sarcoplasmic reticulum calcium pump and plasma membrane Ca2+ pumps revealed by a photoactivatable phospholipidic probe
J. Biol. Chem.
284
4823-4828
2009
Homo sapiens, Oryctolagus cuniculus (P20647)
brenda
Tadini-Buoninsegni, F.; Bartolommei, G.; Moncelli, M.R.; Tal, D.M.; Lewis, D.; Inesi, G.
Effects of high-affinity inhibitors on partial reactions, charge movements, and conformational states of the Ca2+ transport ATPase (sarco-endoplasmic reticulum Ca2+ ATPase)
Mol. Pharmacol.
73
1134-1140
2008
Oryctolagus cuniculus (P04191)
brenda
Sanchez, G.A.; Takara, D.; Alonso, G.L.
Local anesthetics inhibit Ca-ATPase in masticatory muscles
J. Dent. Res.
89
372-377
2010
Oryctolagus cuniculus
brenda
Clausen, J.D.; Andersen, J.P.
Glutamate 90 at the luminal ion gate of sarcoplasmic reticulum Ca2+-ATPase is critical for Ca2+ binding on both sides of the membrane
J. Biol. Chem.
285
20780-20792
2010
Oryctolagus cuniculus (B6CAM1)
brenda
Bartolommei, G.; Tadini-Buoninsegni, F.; Moncelli, M.R.; Gemma, S.; Camodeca, C.; Butini, S.; Campiani, G.; Lewis, D.; Inesi, G.
The Ca2+-ATPase (SERCA1) is inhibited by 4-aminoquinoline derivatives through interference with catalytic activation by Ca2+, whereas the ATPase E2 state remains functional
J. Biol. Chem.
286
38383-38389
2011
Oryctolagus cuniculus (P04191), Oryctolagus cuniculus
brenda
Kumar, S.; Li, C.; Montigny, C.; le Maire, M.; Barth, A.
Conformational changes of recombinant Ca2+-ATPase studied by reaction-induced infrared difference spectroscopy
FEBS J.
280
5398-5407
2013
Oryctolagus cuniculus
brenda
Narumi, R.; Yamamoto, T.; Inoue, A.; Arata, T.
Substrate-induced conformational changes in sarcoplasmic reticulum Ca2+-ATPase probed by surface modification using diethylpyrocarbonate with mass spectrometry
FEBS Lett.
586
3172-3178
2012
Oryctolagus cuniculus
brenda
Bublitz, M.; Musgaard, M.; Poulsen, H.; Thogersen, L.; Olesen, C.; Schiott, B.; Morth, J.; Moller, J.; Nissen, P.
Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase
J. Biol. Chem.
288
10759-10765
2013
Oryctolagus cuniculus (P04191), Oryctolagus cuniculus
brenda
Clausen, J.D.; Holdensen, A.N.; Andersen, J.P.
Critical roles of interdomain interactions for modulatory ATP binding to sarcoplasmic reticulum Ca2+-ATPase
J. Biol. Chem.
289
29123-29134
2014
Oryctolagus cuniculus (P04191)
brenda
Viskupicova, J.; Majekova, M.; Horakova, L.
Inhibition of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA1) by rutin derivatives
J. Muscle Res. Cell Motil.
36
183-194
2015
Oryctolagus cuniculus (P04191)
brenda
Sacchetto, R.; Bertipaglia, I.; Giannetti, S.; Cendron, L.; Mascarello, F.; Damiani, E.; Carafoli, E.; Zanotti, G.
Crystal structure of sarcoplasmic reticulum Ca2+-ATPase (SERCA) from bovine muscle
J. Struct. Biol.
178
38-44
2012
Oryctolagus cuniculus, Bos taurus (Q0VCY0), Bos taurus
brenda
Vargas-Medrano, J.; Sierra-Fonseca, J.; Plenge-Tellechea, L.
1,2-Dichlorobenzene affects the formation of the phosphoenzyme stage during the catalytic cycle of the Ca2+-ATPase from sarcoplasmic reticulum
BMC Biochem.
17
5-5
2016
Oryctolagus cuniculus
brenda
Tatyanenko, L.V.; Khakina, E.A.; Zhilenkov, A.V.; Troshin, P.A.; Dobrokhotova, O.V.; Pikhteleva, I.Y.; Kotelnikov, A.I.
Effects of fullerene derivatives on activity of Ca2+-ATPase of the sarcoplasmic reticulum and cGMP phosphodiesterase
Bull. Exp. Biol. Med.
163
321-325
2017
Oryctolagus cuniculus
brenda
Yonekura, S.; Toyoshima, C.
Mn2+ transport by Ca2+-ATPase of sarcoplasmic reticulum
FEBS Lett.
590
2086-2095
2016
Oryctolagus cuniculus (P04191)
brenda
Yamasaki, K.; Daiho, T.; Danko, S.; Yasuda, S.; Suzuki, H.
Nanodisc-based kinetic assays reveal distinct effects of phospholipid headgroups on the phosphoenzyme transition of sarcoplasmic reticulum Ca2+-ATPase
J. Biol. Chem.
292
20218-20227
2017
Oryctolagus cuniculus (P04191)
brenda