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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+/in
ADP + phosphate + Ca2+/out
ATP + H2O + Ca2+/out
ADP + phosphate + Ca2+/in
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
ATP + H2O + Ca2+[side 1] + H+[side 2]
ADP + phosphate + Ca2+[side 2] + H+[side 1]
-
-
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
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
-
-
-
-
?
CTP + H2O + Ca2+[side 1]
CDP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
GTP + H2O + Ca2+/in
GDP + phosphate + Ca2+/out
-
-
-
?
GTP + H2O + Ca2+[side 1]
GDP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
ITP + H2O + Ca2+[side 1]
IDP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
p-nitrophenyl phosphate + H2O + Ca2+/in
?
-
-
-
-
?
UTP + H2O + Ca2+/in
UDP + phosphate + Ca2+/out
UTP + H2O + Ca2+[side 1]
UDP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
additional information
?
-
ATP + H2O
ADP + phosphate
-
Ca2+-independent ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O + 2 Ca2+[cytoplasm side]
ADP + phosphate + 2 Ca2+[lumen side]
-
-
-
?
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 + 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
-
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
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
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
recombinant enzyme
-
-
?
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 activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
Homarus sp.
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
Homarus sp.
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
656099, 667623, 695512, 696391, 697160, 697167, 697168, 697858, 698973, 700358, 701104 -
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
ATPase activity and Ca2+ transport activity
-
-
?
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
Ca2+-dependent ATPase and ATP-dependent Ca2+ transport activities
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
the enzyme is a plasma membrane calcium pump performing Ca2+-dependent ATPase and ATP-dependent Ca2+ transport reactions
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the PMCA pump uses a molecule of ATP to transport one molecule of Ca2+ from the cytosol to the external environment
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
SERCA1 is responsible for ATPase activity and intermediate reactions, as well as ATP-dependent Ca2+ transport
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
analysis of Ca2+ binding at the two specific transmembrane sites using detergent- and ATP-free enzyme, yielding cooperative isotherms. Calcium occupancy of site I is required to trigger cooperative binding to site II and catalytic activation. Charge transfer and current transients measurements, overview
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
-
-
-
-
?
ATP + H2O + Ca2+/cis
ADP + phosphate + Ca2+/trans
the PMCA pump uses a molecule of ATP to transport one molecule of Ca2+ from the cytosol to the external environment
-
-
?
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
-
-
-
?
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+/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
-
ATPase activity and Ca2+ uptake into artificial proteoliposomes activity
-
-
?
ATP + H2O + Ca2+/in
ADP + phosphate + Ca2+/out
-
-
-
-
?
ATP + H2O + Ca2+/in
ADP + phosphate + Ca2+/out
-
plasma-membrane Ca2+-ATPase is a calcium pump that exports Ca2+ from the cytosol to the extracellular environment of eukaryotic cells and thus maintain overall Ca2+ homoeostasis and provide local control of intracellular Ca2+ signalling
-
-
?
ATP + H2O + Ca2+/out
?
-
responsible for Ca2+ uptake into the alveolar sac
-
-
?
ATP + H2O + Ca2+/out
?
-
responsible for Ca2+ uptake into the alveolar sac
-
-
?
ATP + H2O + Ca2+/out
?
-
high affinity (Ca2+-Mg2+)-ATPase is responsible for Ca2+ transport
-
-
?
ATP + H2O + Ca2+/out
?
-
filling of the Ca2+ pool in the endoplasmic reticulum
-
-
?
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
Dorytheutis plei
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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+/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
Pigeon
-
-
-
?
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
-
-
-
?
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+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
733067, 733277, 733466, 734224, 734517, 735113, 748570, 749980, 750486, 750998, 751700, 752192 -
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
Plasmodium falciparum isolate K1
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
best substrate
-
-
?
ATP + H2O + Ca2+[side 1]
ADP + phosphate + Ca2+[side 2]
-
-
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
-
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
ATP + H2O + Mn2+/cis
ADP + phosphate + Mn2+/trans
Mn2+-dependent ATPase and ATP-dependent Mn2+ transport activities
-
-
?
UTP + H2O + Ca2+/in
UDP + phosphate + Ca2+/out
-
-
-
?
UTP + H2O + Ca2+/in
UDP + phosphate + Ca2+/out
-
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
isoform ECA3 function cannot be replaced by an endoplasmic reticulum-associated isoform ECA1, ECA3 is also important for the detoxification of excess Mn2+, isoform ECA3 is a distinct Ca2+/Mn2+ pump critical for Ca2+-enhanced root growth
-
-
?
additional information
?
-
-
ER-type Ca2+-ATPases show a strong preference for ATP as substrate. Conversely, auto-inhibited Ca2+-ATPases are able to use ITP or GTP as an alternative to ATP
-
-
?
additional information
?
-
the Arabidopsis thaliana endoplasmic reticulum-localized Ca2+-ATPase, ECA1, with homology to PMR1, can also transport Mn2+. Molecular determinants of the Mn2+ specificity of transport proteins
-
-
-
additional information
?
-
-
the enzyme is involved in calcium and maganese homeostasis
-
-
?
additional information
?
-
-
the P-type calcium ATPase is important for calcium/manganese homeostasis and oxidative stress response
-
-
?
additional information
?
-
the enzyme is a P-type Ca2+/Mn2+-ATPase involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme is a P-type Ca2+/Mn2+-ATPase involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity, functional regulation by phospholamban
-
-
?
additional information
?
-
Homarus sp.
-
the enzyme is involved in the transepithelial Ca2+ flow in hepatopancreas of lobster acting as an ATP-driven Ca2+ pump in conjunction with a Na+/Ca2+ antiporter in the basolateral cell region, Ca2+ transport mechanism by endoplasmic reticular vesicles, overview
-
-
?
additional information
?
-
-
the Ca2+,Mn2+-ATPase SPCA2 is involved in the secretory pathway
-
-
?
additional information
?
-
-
the enzyme is important in the secretory pathway
-
-
?
additional information
?
-
the enzyme is important in the secretory pathway
-
-
?
additional information
?
-
-
dissection of the functional differences between secretory pathway Ca2+/Mn2+-ATPase isoenzymes SPCA 1 and 2
-
-
?
additional information
?
-
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
-
-
?
additional information
?
-
-
the activity of the plasma membrane Ca2+-pump decreases steeply throughout the 120 days lifespan of normal human red blood cells, the Ca2+ pump is a major regulator of Ca2+ homeostasis in all cells
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PMCA2 also has an important role in the regulation of Ca2+ concentration in the milk
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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
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interaction of Ca2+-ATPase with phospholamban is involved in regulation of heart contractility, overview
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the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
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interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals, overview
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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
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SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
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SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
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SERCA 2 type Ca2+-ATPases dominate in red muscle and blood platelets where this heat flux is not so central
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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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additional information
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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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additional information
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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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additional information
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the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
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additional information
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the enzyme performs ATP-dependent Ca2+ transport and Ca2+-dependent ATPase activity
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additional information
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the enzyme plays a significant role in cellular Ca2+ homeostasis
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additional information
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the enzyme binds calmodulin with high affinity
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the enzyme is responsible for the Ca2+ sequestering
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(12S,12aR)-3-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
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(1R,9aR)-9-[2-[(4-fluorobenzyl)oxy]ethyl]-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,6R,9aS)-3,6-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl phenylacetate
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(1S,9aR)-1-methoxy-3-methyl-9-[2-(phenylperoxy)ethyl]octahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,9aR)-1-methoxy-3-methyl-9-[2-(prop-2-en-1-yloxy)ethyl]octahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,9aR)-9-[2-(benzyloxy)ethyl]-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,9aS)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(1S,9aS)-1-[2-(benzyloxy)ethyl]-1,3,9-trimethyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(2Z)-2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enethioamide
-
-
(3R,5aS,6R,8aS,12aS)-11-benzyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-(2-methylbutyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-(2-phenylethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-(3-phenylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-(4-methylbenzyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-11-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3-butyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3-ethyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-3-[3-(4-chlorophenyl)propyl]-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-6-methyl-3-(3-phenylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,12aS)-6-methyl-3-propyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12aR)-3,9-dibutyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12aR)-9-butyl-3-ethyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12aR)-9-butyl-3-[3-(4-chlorophenyl)propyl]-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12aR)-9-butyl-6-methyl-3-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3R,5aS,6R,8aS,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
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(3R,5aS,6R,8aS,9R,12S,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
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(3R,6R,9R,12R,12aR)-6,9-dimethyl-10-(2,2,2-trifluoroethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-9-ol
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(3R,6R,9S,12R,12aR)-10-ethoxy-6,9-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-9-ol
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(3R,6R,9S,12R,12aR)-6,9-dimethyl-10-(2,2,2-trifluoroethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-9-ol
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(3R,6R,9S,12R,12aR)-6,9-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,10-diol
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(3S,5aR,6S,8aR,9R,12S,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl N-[(2-methylpropoxy)carbonyl]-b-alaninate
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(3S,5aS,6R,8aS,12aS)-6-methyl-3-(2-methylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3S,5aS,6R,8aS,12aS)-6-methyl-3-(2-phenylethyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3S,5aS,6R,8aS,9R,12aR)-9-butyl-6-methyl-3-(2-phenylethyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(3S,6R,12R,12aS)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
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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
-
(4aS)-3,3-diethylhexahydro-6H-[1,2,4]trioxino[6,5-j]isochromen-6-one
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(4aS)-3,3-dimethylhexahydro-6H-[1,2,4]trioxino[6,5-j]isochromen-6-one
-
(4aS)-hexahydro-6H-[1,2,4]trioxino[6,5-j]isochromen-6-one
-
(5S,6R,9R,10S,12R,12aS)-10-ethoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-5-ol
-
(6'R,12'S,12a'R)-3',6'-dimethyl-3',4',5',5a',6',7',8',8a'-octahydrospiro[cyclopent-3-ene-1,9'-[1,2,11,13]tetraoxa[3,12]epoxy[1,2]dioxepino[4,3-i]isochromen]-10'-one
-
(6'R,12'S,12a'R)-3',6'-dimethyloctahydrospiro[1,3-dioxolane-2,9'-[3,12]epoxy[1,2]dioxepino[4,3-i]isochromen]-10'-one
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(6R,10R,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl hydroperoxide
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(6R,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-ol
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(6R,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
-
(6R,10S,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
-
(6R,12aS)-11-(4-chlorobenzyl)-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
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(6R,12aS)-11-acetyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-11-benzyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-(2-phenylethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-(3-phenylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-(pyridin-2-ylmethyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-(thiophen-2-yl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12aS)-3,6-dimethyl-11-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-10(3H)-one
-
(6R,12R,12aR)-3,6-dimethyl-9-methylidenedecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl hydroperoxide
-
(6R,12R,12aS)-3-butyl-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-3-ethyl-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-3-[3-(4-chlorophenyl)propyl]-6-methyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-6-methyl-3-(2-methylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-6-methyl-3-(4-phenylbutyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12R,12aS)-6-methyl-3-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,12S,12aS)-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,12S,12aS)-3-ethyl-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,12S,12aS)-6-methyl-3-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,12S,12aS)-6-methyl-3-propyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,8aR,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,8aR,9R,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,8aR,9R,12S,12aR)-9-bromo-9-(bromomethyl)-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,8aS,9S,10R,12R,12aR)-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,10-diol
-
(6R,8aS,9Z,12S,12aR)-9-ethylidene-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9aS)-3,6-dimethyloctahydro-3,9a-epidioxy-2-benzoxepine
-
(6R,9R,12R,12aR)-10-(tert-butylperoxy)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-10-ethoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-10-ethoxy-3,6-dimethyl-9-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-10-ethoxy-9-ethyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-10-methoxy-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-ol
-
(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-(3-phenylpropyl)decahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-pentyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6-dimethyl-9-propyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
-
(6R,9R,12R,12aR)-9-butyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12R,12aR)-9-ethyl-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9R,12S,12aR)-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-3,4,4',5,5',5a,6,7,8,8a-decahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,3'-pyrazol]-10-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(2-methylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(2-phenylethyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(3-phenylpropyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(prop-2-en-1-yl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-(propan-2-yl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-3,6-dimethyl-9-pentyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-butyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-butyl-6-methyl-3-(4-phenylbutyl)octahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-ethyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-hexyl-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9R,12S,12aR)-9-[3-(4-chlorophenyl)propyl]-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9S,10R,12R,12aR)-3,6-dimethyloctahydrospiro[3,12-epoxy[1,2]dioxepino[4,3-i]isochromene-9,2'-oxiran]-10-yl hydroperoxide
-
(6R,9S,11aR)-3,6,9-trimethyloctahydro-3H-3,11-epoxyfuro[3,4-j][1,2]benzodioxepine
-
(6R,9S,12R,12aR)-9-bromo-3,6,9-trimethyl-N-phenyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-amine
-
(6R,9S,12R,12aR)-9-bromo-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6R,9S,12S,12aR)-9-[(1E)-but-1-en-1-yl]-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6R,9S,12S,12aR)-9-[(2E)-but-2-en-1-yl]-3,6-dimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10(3H)-one
-
(6S,7S,10S,12aS)-10-ethoxy-7-fluoro-3,6,7-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(6S,7S,10S,12R,12aS)-10-ethoxy-3,6-dimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-7-ol
-
(6S,9R,10S,12aS)-10-ethoxy-3,6,9-trimethyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-7(3H)-one
-
(6S,9R,10S,12aS)-10-ethoxy-7,7-difluoro-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromene
-
(7R,12aR)-7,10-dimethyldodecahydro-2H-10,13-epoxy[1,2]dioxepino[4,3-i]pyrano[2,3-c]isochromene
-
(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
1,5-bis(4-methoxyphenyl)-6,7-dioxabicyclo[3.2.2]nonane
-
1,5-diphenyl-3,6,7-trioxabicyclo[3.2.2]nonane
-
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
-
1-[(6R)-3,3,6-trimethyloctahydro-9aH-1,2-benzodioxepin-9a-yl]ethanone
-
2,2',2''-methanetriyltris(4-tert-butylphenol)
-
2,2'-methanediylbis(4-tert-butylphenol)
-
2,3-bis[(2-hydroxyethyl)sulfanyl]naphthalene-1,4-dione
-
-
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)-1,4-benzohydroquinone
-
-
2,5-di(tert-butyl)hydroquinone
micromolar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
2,5-di-tert-butyl-1,4-dihydroxybenzene
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-(dimethylamino)ethyl 4-(2-oxo-2-[[(3S,5aR,6S,8aR,9R,12S,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]ethyl)benzoate
-
2-(dimethylamino)ethyl 4-[([2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl]peroxy)methyl]benzoate
-
2-cyclooctylbenzene-1,4-diol
-
2-phenyl-1,2-benzoselenazol-3(2H)-one
-
-
2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl diethylcarbamate
-
2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl diphenylcarbamate
-
2-[(1S,9aS)-1,3,9-trimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
-
2-[(1S,9aS)-1,3-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
-
2-[(1S,9aS)-3,9-dimethyloctahydro-3,9a-epidioxy-2-benzoxepin-1(1H)-yl]ethanol
-
2-[(cyclopropylcarbonyl)amino]-4,5-dimethylthiophene-3-carboxamide
-
-
3-(1,1-diphenylethyl)cyclopentanol
-
3-[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]propan-1-ol
-
4,4'-butane-2,2-diylbis(2-methylphenol)
-
4,4'-butane-2,3-diyldiphenol
-
4,4'-diisothiocyano-2,2'-stilbenedisulfonic acid
-
-
4,4'-propane-2,2-diylbis(2,6-dimethylphenol)
-
4,5-dibenzylbenzene-1,2-diol
-
4,5-dimethyl-2-([[5-methyl-2-(propan-2-yl)phenoxy]acetyl]amino)thiophene-3-carboxamide
-
-
4-(2-[2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethoxy]ethyl)pyridine
-
4-(7-methyloctyl)phenol
-
4-([2-[(1R,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethoxy]methyl)pyrimidine
-
4-([[(3R,5aS,6R,8aS,9R,10S,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]methyl)benzoic acid
-
5(6)-carboxyeosin diacetate
-
-
5-chloro-N-(3,5-dimethoxyphenyl)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-methoxybenzamide
-
-
6-amino-2-(hex-1-yn-1-yl)-9H-purin-9-yl-beta-D-N-ethylribofuranoic amide
-
-
6-tert-butyl-2,3-dihydro-1H-inden-5-ol
-
6-[(3R,5aS,6R,8aS,12aS)-3,6-dimethyl-10-oxodecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isoquinolin-11(12H)-yl]hexanoic acid
-
7-chloro-4-(piperazin-1-yl)quinoline
-
aluminium fluoride
-
the inhibition by aluminium fluoride is dependend on Mg2+ concentration
amyloid beta-peptide
-
the addition of amyloid beta-peptide to normal brain decreases the PMCA activity resulting in the same Ca2+ dependency as that seen in Alzheimer's disease brain, whereas the addition of amyloid beta-peptide to Alzheimer's disease brain has no effect on PMCA activity, in the absence of cholesterol, the level of inhibition of cerebrum PMCA is 60%, but levels of inhibition decreases with increasing concentrations of cholesterol
-
amyloid beta-peptide 1-40
-
-
amyloid beta-peptide 25-35
-
beryllium fluoride
-
the inhibition by beryllium fluoride is dependend on Mg2+ concentration
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
calmodulin antagonist compound 48/80
-
inhibits phosphatase activity
chlorpromazine
-
non-competitive inhibition, complete inhibition at 1 mM
D-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol
-
-
detergent C12E8
-
inhibition of mutant D813A/D818A
eosin Y
-
auto-inhibited Ca2+-ATPases are particularly sensitive to inhibition by eosin Y
ethyl 3-[(3S,5aS,6R,8aS,12aS)-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl 3-[(3S,5aS,6R,8aS,9R,12aR)-9-butyl-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl 3-[(6R,12R,12aS)-6-methyloctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl 3-[(6R,12S,12aS)-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl 3-[(6R,9R,12S,12aR)-9-butyl-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propanoate
-
ethyl [[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]acetate
-
fluoroglycofen
-
i.e. O-[5-(2-chloro-alpha,alpha,alpha-trifluoro-of-toluene-oxy)-2-nitro-benzoyl]-hydroxyethyl, a high concentration of fluoroglycofen (37.5 g ai ha-1) decreases the enzyme activity in grape leaves
Hg2+
-
0.25 mM, 50% inhibition
hydroxylamine
-
the enzyme is sensitive to treatment with hydroxylamine
lidocaine
-
inhibition by lidocaine is not competitive with respect to the specific transport and catalytic sites of the enzyme
magnesium fluoride
-
the inhibition by magnesium fluoride is dependend on Mg2+ concentration
methyl 2-methyl-3-[[(3R,5aS,6R,8aS,9R,10R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 2-methyl-3-[[(6R,9R,10R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 2-methyl-3-[[(6R,9R,10S,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 2-[[(6R,9R,10R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 2-[[(6R,9R,10S,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 3-[[(3R,5aS,6R,8aS,9R,10R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]butanoate
-
methyl 3-[[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]propanoate
-
methyl 4-(2-oxo-2-[[(3S,5aR,6S,8aR,9R,12S,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]ethyl)benzoate
-
methyl 4-([[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]methyl)benzoate
-
methyl 4-[[(6R,9R,12R,12aR)-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]oxy]butanoate
-
methyl [(4-tert-butylbenzoyl)amino]acetate
-
-
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-4-(azido-2-nitrophenyl)-2-aminoethylsulfonate
-
-
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
N-[(6R,9R,12R,12aR)-9-bromo-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]pyridin-2-amine
-
N-[(6R,9S,12R,12aR)-9-bromo-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]-1,3-thiazol-2-amine
-
N-[(6R,9S,12R,12aR)-9-bromo-3,6,9-trimethyldecahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-10-yl]pyridin-2-amine
-
Ni2+
-
1 mM, 28% inhibition
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
peptide C28
-
peptide C28 is a peptide that prevents activation of PMCA by calmodulin
-
phosphatidylcholine
-
native PMCA from erythrocytes in mixed micelles of phosphatidylcholine-detergent has 30% of its maximal activity, while the recombinant PMCA enzyme is nearly inactive, increasing the phosphatidylcholine content of the micelles does not increase the activity of recombinant PMCA but the activity in the presence of phosphatidylcholine improves by partially removing the detergent
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
-
-
ruthenium red
-
slight inhibition
rutin 4'''-O-arachidonate
-
rutin 4'''-O-linolenate
-
Sodium fluoride
-
the inhibition by magnesium fluoride is dependend on Mg2+ concentration. The enzyme is totally inhibited by NaF at total Mg2+ concentrations higher than 3.5 mM
Sodium vanadate
-
slight inhibition
tert-butyl [(1E)-1-([2-[(1S,9aR)-1-methoxy-3-methyloctahydro-3,9a-epidioxy-2-benzoxepin-9(1H)-yl]ethyl]peroxy)ethylidene]carbamate
-
tert-butylhydroquinone
-
-
tetrabromobisphenol A
-
can inhibit SERCA at low concentrations (IC50, 0.0004-0.0012 mM)
[(dihydroindenyl)oxy]acetic acid
-
DIOA
[3-[(6R,9R,12S,12aR)-9-butyl-6-methyl-10-oxooctahydro-3,12-epoxy[1,2]dioxepino[4,3-i]isochromen-3(4H)-yl]propyl]phenylphosphinous chloride
-
2,5-di-tert-butyl-1,4-dihydroxybenzene
-
inhibitory effects on wild-type and mutant enzymes, overview
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
amyloid beta-peptide 25-35
-
a maximum inhibition of 75% is observed with 0.0025 mM amyloid beta-peptide 25-35 for PMCA reconstituted in phosphatidylcholine.
-
amyloid beta-peptide 25-35
the activity of overexpressed PMCA4 in a microsomal fraction of the HEK-293 cells is inhibited by amyloid beta-peptide 25-35, a slight inhibition of the activity of PMCA3 is observed
-
artemisinin
-
artemisinin
Ca2+-ATPase and Golgi localized Pmr1p appears to be targets for artemisinin
artesunate
-
Ca2+
-
-
Ca2+
-
above 0.1 mM, Ca2+-dependent ATPase
Calmidazolium
-
-
carboxyeosin
-
-
carboxyeosin
-
blocker of PMCA
Cd2+
-
1 mM, 39% inhibition
Cd2+
-
enzyme activity shows a gradual decrease in post larvae on exposure to 0.12 and 0.24 ppm cadmium
Cu2+
Homarus sp.
-
reduces the Ca2+ content in the cytosol
Cu2+
-
0.5 mM, 50% inhibition
cyclopiazonic acid
-
inhibitor of ER-type Ca2+-ATPases
cyclopiazonic acid
-
specific inhibitor
cyclopiazonic acid
nanomalar inhibitor of SERCA, inhibits Ca2+ binding and catalytic activation
cyclopiazonic acid
-
very potent inhibitor
cyclopiazonic acid
-
weak
cyclopiazonic acid
highly sensitive to the specific inhibitor cyclopiazonic acid
dihydroartemisinin
-
EGTA
-
-
erythrosin B
-
auto-inhibited Ca2+-ATPases are particularly sensitive to inhibition by erythrosin B
La3+
-
-
La3+
-
prevents the Mg2+-dependent transition E1P->E2P, acting noncompetitively with respect to Ca2+ and ATP
Mg2+
-
competitive Mg2+ binding can occur at Ca2+ binding site I but not at site II
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
orthovanadate
-
-
orthovanadate
-
the Ca2+ pump is inhibited by orthovanadate (0.1 mM) once sufficient Ca2+ accumulation has occurred
orthovanadate
-
50% inhibition at 0.13 mM
phospholamban
-
complex formation with the recombinant SERCA2a in transfected insect cells, regulatory function, overiew
-
phospholamban
-
phospholamban inhibits SERCA2a activity in its dephosphorylated state
-
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
Homarus sp.
-
-
thapsigargin
-
inhibits SERCA activity
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
thapsigargin
highly specific inhibitor
thapsigargin
-
SERCA is inhibited by 0.001 mM thapsigargin
thapsigargin
-
no effect up to 0.005 mM
thapsigargin
only mildly sensitive to the ER-type pump inhibitor thapsigargin
thapsigargin
-
specific inhibitor, complete inhibition at 50 nM
thapsigargin
-
80% inhibition at 0.003 mM
vanadate
-
-
vanadate
inhibits the phosphorylation reaction; inhibits the phosphorylation reaction
vanadate
-
inhibits the phosphorylation reaction
vanadate
potent inhibitor
Zn2+
Homarus sp.
-
reduces the Ca2+ content in the cytosol
Zn2+
-
1 mM, 50% inhibition
additional information
-
in the resting state, the plant plasma-membrane Ca2+-ATPase is autoinhibited by binding of its N-terminal tail to two major intracellular loops. Activation requires the binding of calcium-bound calmodulin to this tail and a conformational change that displaces the autoinhibitory tail from the catalytic domain
-
additional information
-
PMCA is insensitive to increases in membrane potential
-
additional information
-
the Na+/Ca2+ exchanger plays a minimal role in the cell Ca2+-fluxes
-
additional information
-
the enzyme has an autoinhibitory domain which is coupled to the ATP binding domain, oxidative modification alters the interaction and inhibits the enzyme, proteolysis pattern of inactive PMCAox by chymotrypsin, overview
-
additional information
the Ca2+ and Mn2+ transport of SPCA2 is insensitive to thapsigargin inhibition
-
additional information
-
the Ca2+ and Mn2+ transport of SPCA2 is insensitive to thapsigargin inhibition
-
additional information
-
SERCA protein expression is decreased by inhibition of cystic fibrosis transmembrane regulator function with the specific cystic fibrosis transmembrane regulator inhibitor CFTRinh172
-
additional information
-
the function of recombinant PMCA is highly sensitive to delipidation
-
additional information
-
glycation of a lysine residue near the catalytic site of the pump ATPase has a powerful inhibitory effect, in intact cells the Ca2+ pump is protected from glycation-induced inactivation
-
additional information
-
no inhibition of isoforms PMCA4 and PMCA2 is observed with the amyloid beta-peptide 25-35. The addition of 0.0025 mM amyloid beta-peptide 25-35 to Alzheimer's disease brain has no effect on PMCA activity. No effect of amyloid beta-peptides is seen on SERCA or SPCA activity in either control or Alzheimer's disease brains
-
additional information
-
PCA1 contains a N-terminal autoinhibitory domain
-
additional information
artemisinins have been widely used to treat both Plasmodium falciparum and Plasmodium vivax infections due to their high clinical efficacy (immediate onset and rapid parasite clearance) and minimal side effects. Moreover, artemisinins remain highly effective against malaria parasites that show resistance to other classes of antimalarial medicine. Combinations of artemisinin and other antimalarial drugs are utilized clinically to enhance effectiveness and minimize the development of artemisinin resistance in Plasmodium species. Despite this strategy, artemisinin-resistant Plasmodium isolates have emerged
-
additional information
-
artemisinins have been widely used to treat both Plasmodium falciparum and Plasmodium vivax infections due to their high clinical efficacy (immediate onset and rapid parasite clearance) and minimal side effects. Moreover, artemisinins remain highly effective against malaria parasites that show resistance to other classes of antimalarial medicine. Combinations of artemisinin and other antimalarial drugs are utilized clinically to enhance effectiveness and minimize the development of artemisinin resistance in Plasmodium species. Despite this strategy, artemisinin-resistant Plasmodium isolates have emerged
-
additional information
-
the Ca2+ transporting function of SERCA2a is decreased by about 18% 1 week, 1 month, and 3 months after myocardial infarction, while PMCA1, 2, and 4 mRNAs are unchanged in the ventricular muscle 3 months after myocardial infarction
-
additional information
-
PMCA is inhibited by acutely lowering extracellular proton concentration (pH raised to 9.0)
-
additional information
artemisinin resistance in pmr1DELTA cells is not caused by alteration in the localization or accumulation of the multidrug transporter Pdr5p as well as not by association between defects in calcium homeostasis or protein glycosylation and sensitivity to artemisinin
-
additional information
-
artemisinin resistance in pmr1DELTA cells is not caused by alteration in the localization or accumulation of the multidrug transporter Pdr5p as well as not by association between defects in calcium homeostasis or protein glycosylation and sensitivity to artemisinin
-
additional information
no inhibition of isoforms PMCA4 and PMCA2 is observed with the amyloid beta-peptide 25-35, 0.0025 mM amyloid beta-peptide 25-35 has no effect on the activity of PMCA purified from cerebellum
-
additional information
-
no inhibition of isoforms PMCA4 and PMCA2 is observed with the amyloid beta-peptide 25-35, 0.0025 mM amyloid beta-peptide 25-35 has no effect on the activity of PMCA purified from cerebellum
-
additional information
the enzyme is not significantly inhibited by oligomycin
-
additional information
the enzyme possesses an autoinhibitory domain at its C-terminal tail
-
additional information
-
the enzyme possesses an autoinhibitory domain at its C-terminal tail
-
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0.007
(2Z)-2-cyano-3-(3,4-dihydroxyphenyl)prop-2-enethioamide
Plasmodium falciparum
-
at pH 7.5 and 25°C
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)
0.001
2,3-bis[(2-hydroxyethyl)sulfanyl]naphthalene-1,4-dione
Plasmodium falciparum
-
at pH 7.5 and 25°C
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)
0.065
2,5-di(tert-butyl)-1,4-benzohydroquinone
Plasmodium falciparum
-
at pH 7.5 and 25°C
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)
0.001
2-phenyl-1,2-benzoselenazol-3(2H)-one
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.0031
2-[(cyclopropylcarbonyl)amino]-4,5-dimethylthiophene-3-carboxamide
Plasmodium falciparum
-
at pH 7.5 and 25°C
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)
0.0011
4,5-dimethyl-2-([[5-methyl-2-(propan-2-yl)phenoxy]acetyl]amino)thiophene-3-carboxamide
Plasmodium falciparum
-
at pH 7.5 and 25°C
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)
0.003
5-chloro-N-(3,5-dimethoxyphenyl)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-methoxybenzamide
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.0085
6-amino-2-(hex-1-yn-1-yl)-9H-purin-9-yl-beta-D-N-ethylribofuranoic amide
Plasmodium falciparum
-
at pH 7.5 and 25°C
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)
0.0025
amyloid beta-peptide 25-35
Sus scrofa
-
-
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
0.085 - 0.42
chlorpromazine
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
0.00016 - 0.0004
cyclopiazonic acid
0.0036
eosin
Solanum lycopersicum
in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37°C
0.0012
methyl [(4-tert-butylbenzoyl)amino]acetate
Plasmodium falciparum
-
at pH 7.5 and 25°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
0.000635 - 0.15
thapsigargin
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
0.085
chlorpromazine
Homo sapiens
-
trypsin-activated enzyme, at pH 7.2 and 25°C
0.15
chlorpromazine
Homo sapiens
-
native enzyme in the presence of 0.002 mg/ml calmodulin, at pH 7.2 and 25°C
0.42
chlorpromazine
Homo sapiens
-
native enzyme, at pH 7.2 and 25°C
0.00016
cyclopiazonic acid
Solanum lycopersicum
in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37°C
0.0004
cyclopiazonic acid
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.000635
thapsigargin
Solanum lycopersicum
recombinant enzyme expressed in Saccharomyces cerevisiae strain HI227, in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37°C
0.00095
thapsigargin
Solanum lycopersicum
recombinant enzyme expressed in Saccharomyces cerevisiae strain K616, in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37°C
0.15
thapsigargin
Plasmodium falciparum
-
at pH 7.5 and 25°C
0.0057
vanadate
Solanum lycopersicum
in 1 mM EGTA, 130 mM NaCl, 3 mM MgCl2, at 37°C
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
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evolution
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6
evolution
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6. Pmr1p is a key transporter for uptake of Ca2+ into the Golgi, which is important for maintaining the Ca2+ homeostasis of yeast cells
evolution
-
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6
-
evolution
-
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6. Pmr1p is a key transporter for uptake of Ca2+ into the Golgi, which is important for maintaining the Ca2+ homeostasis of yeast cells
-
evolution
Plasmodium falciparum isolate K1
-
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6
-
malfunction
-
knock-out mutants of isoform ACA9 displays reduced growth of pollen tubes, with high frequency of aborted fertilization leading to a 3fold reduction in seed set. Knock-out mutants of isoforms ACA8 or ACA10 do not have an altered phenotype, with a noticeable exception: knock-out of ACA10 in a genotype containing a naturally occurring dominant allele of an unlinked gene causes altered adult vegetative development and the formation of floral clusters. Isoform ECA1 knock-out mutant is indistinguishable from the wild type, but it clearly shows reduced root growth and toxicity symptoms when exposed to 0.5 mM Mn2+. An ECA3 knock-out mutant is not more sensitive than the wild type to Mn2+ toxicity, but rather requires higher Mn2+ concentrations for growth. Both isoform ECA1 and ECA3 knock-out mutants have slightly altered Ca2+ sensitivity
malfunction
-
after injection of thapsigargin to block enzyme activity, silkworms show a silk-spinning deficiency (30% of silkworms cannot spin normally and another 25% constructes abnormal cocoons) and their cocoons have higher calcium content compared to that of controls
malfunction
-
age-associated loss in PMCA activity results in part from changes in the lipid environment of this Ca2+ transporter
malfunction
-
gene disruption causes severe defects in glycosylation of the endoplasmic reticulum (ER)-localized protein Cdc101 and secretory acid phosphatase, and a decrease in expression of SEC61 which encodes an important ER protein. Moreover, the enzyme deletion mutant shows increased sensitivity to cell wall stresses, abnormal cell wall composition, delayed cell wall reconstruction and decreased flocculation and adherence
malfunction
-
isoform PMCA2 or PMCA3 knock-down delays Ca2+ clearance and partially attenuates cellular acidification during KCl-stimulated Ca2+ influx
malfunction
-
plasma membrane Ca2+-ATPase 1 deficiency increases susceptibility to atrial tachyarrhythmia in Langendorff-perfused hearts under stress conditions. Enzyme deficiency produces instabilities in membrane potentials and Ca2+ handling in atrial myocytes
malfunction
-
enzyme function is not altered in muscle of patients with myotonic dystrophy and with hypothyroid myopathy
malfunction
-
silencing of isoform PMCA2 reduces MDA-MB-231 breast cancer cell proliferation, whereas silencing of the related isoforms PMCA1 and PMCA4 has no effect. PMCA2 silencing also sensitizes MDA-MB-231 cells to doxorubicin
malfunction
a T-DNA knockout of ECA1, grown on high-Mn media, displays a strong stress phenotype when compared to wild-type plants. This phenotype includes a significant reduction in fresh weight, dramatic leaf chlorosis, a significant inhibition of leaf expansion and root elongation, and a loss of root hair tip growth. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrated a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants. ILR2 might act as a regulator of Mn2+ transport, possibly acting on Mn2+ efflux from the cell mediated by either an ATPase or an ABC transporter
malfunction
cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1D yeast and artemisinin exposure does not enhance ROS accumulation. Yeast deleted for PMR1 are known to accumulate excess manganese ions that can function as ROS-scavenging molecules. Loss-of-function mutations in Pmr1p in yeast cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage, artemisinin resistance in pmr1DELTA cells. The loss of function in Pmr1p results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
malfunction
loss-of-function mutations in PfATP6 in Plasmodium falciparum cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage. The loss of function in PfATP6 results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
malfunction
the pmr1 knockout (DELTApmr1) cells exhibit hypersensitivity to EGTA. The EGTA-hypersensitive phenotype of DELTApmr1 leads to the identification of pdt1+ gene, which encodes an Nramp-related metal transporter. The DELTApmr1 cells show round cell morphology. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
malfunction
-
loss-of-function mutations in PfATP6 in Plasmodium falciparum cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage. The loss of function in PfATP6 results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
-
malfunction
-
the pmr1 knockout (DELTApmr1) cells exhibit hypersensitivity to EGTA. The EGTA-hypersensitive phenotype of DELTApmr1 leads to the identification of pdt1+ gene, which encodes an Nramp-related metal transporter. The DELTApmr1 cells show round cell morphology. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
-
malfunction
-
cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1D yeast and artemisinin exposure does not enhance ROS accumulation. Yeast deleted for PMR1 are known to accumulate excess manganese ions that can function as ROS-scavenging molecules. Loss-of-function mutations in Pmr1p in yeast cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage, artemisinin resistance in pmr1DELTA cells. The loss of function in Pmr1p results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
-
malfunction
Plasmodium falciparum isolate K1
-
loss-of-function mutations in PfATP6 in Plasmodium falciparum cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage. The loss of function in PfATP6 results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
-
metabolism
-
Ca2+ removal by the enzyme influences the propensity for stimulus-evoked Ca2+-induced Ca2+ release by adjusting the amount of Ca2+ available for mitochondrial Ca2+ uptake
metabolism
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
metabolism
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
metabolism
-
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
-
physiological function
-
plasma-membrane Ca2+-ATPases, PMCAs, are high-affinity calcium pumps that expel Ca2+ from eukaryotic cells to maintain overall Ca2+ homoeostasis and to provide local control of intracellular Ca2+ signalling. They are of major physiological importance, with different isoforms being essential, for example, for presynaptic and postsynaptic Ca2+ regulation in neurons, feedback signalling in the heart and sperm motility
physiological function
-
sarcoplasmic reticulum Ca-ATPase is a membrane-bound protein which transports calcium ions from the myoplasm to the reticulum lumen at the expense of ATP hydrolysis, leading to muscle relaxation
physiological function
-
both endomembrane P2A and P2B Ca2+-ATPases play significant roles in adaptive responses to oxidative stress by removing excessive Ca2+ from the cytosol. Plasma membrane P2B type pumps play no major role in removing excess Ca2+ from the cytosol under oxidative stress conditions
physiological function
-
Ca2+-ATPases use the energy of ATP hydrolysis to pump Ca2+ from the cytoplasm into intracellular compartments or into the apoplast. Ca2+-ATPases play an important role in maintenance of cytoplasmic Ca2+ homeostasis. Isoform ECA3 may also play an essential role in Mn2+ nutrition. Plasma membrane-localized auto-inhibited Ca2+-ATPases are also involved in the response to pathogens, hormonal regulation, salt stress, and cold stress
physiological function
enzyme overexpression decreases [Ca2+] in the cytosol, the endoplasmic reticulum (ER), and the mitochondria and activates the inositol-requiring transmembrane kinase and endonuclease 1alpha-spliced X-box binding protein 1 but inhibits the PRKR-like ER kinase-eIF2alpha and the activation of transcription factor 6-immunoglobulin heavy chain binding protein pathways of the ER-unfolded protein response. Isoform PMCA2 overexpression depletes cytosolic, ER and mitochondrial Ca2+ stores and induces apoptosis via the mitochondrial pathway. PMCA2-overexpressing cells also display increased levels of caspase-3 cleavage
physiological function
isoform SERCA2b plays an important role in dysregulated glucose and lipid homeostasis in the liver of obese mice. Overexpression of isoform SERCA2b in the liver of obese mice significantly reduces the lipogenic gene expression and the triglyceride content in the liver and reduces steatohepatitis. Increasing the levels of isoform SERCA2b greatly reduces endoplasmic reticulum stress in the liver, increases glucose tolerance, and establishes euglycemia in severely obese and diabetic mice. Isoform SERCA2b can increase endoplasmic reticulum folding capacity
physiological function
-
isoforms PMCA2 and PMCA3 are mainly responsible for transport of protons to the intracellular milieu and the regulation of cellular pH
physiological function
-
sarcoplasmic reticulum Ca2+ ATPase pump is a major regulator of glucose transport in the healthy and diabetic heart. Cardiac-specific enzyme expression increases active cell-surface GLUT4 and glucose uptake in the myocardium, as well as whole body glucose tolerance. The enzyme regulates cardiac GLUT4 translocation
physiological function
the combination of the functional attributes of both PMCA4 variants leads to heightened efficiency of the pump in the maintenance of Ca2+ homeostasis, which is crucial for normal motility and male fertility
physiological function
-
the enzyme has a key function in calcium transportation in anterior silk gland that is related to maintaining a suitable ionic environment. This ionic environment with a proper Ca2+ concentration is crucial for the formation of silk fibers with favorable mechanical performances
physiological function
-
the enzyme is responsible for intracellular Ca2+ homeostasis. Enzyme uncoupling of Ca2+ transport from ATP hydrolysis by sarcolipin increases heat production implicating sarcolipin-enzyme interaction in muscle thermogenesis
physiological function
-
the enzyme plays key roles in maintenance of cellular Ca2+ homeostasis, morphogenesis and virulence and is essential for endoplasmic reticulum (ER) functions and consequent cell wall integrity implicating a role of ER Ca2+ homeostasis in Candida albicans physiology
physiological function
-
the limited ability of isoform PMCA2 to extrude the Ca2+ load through mechanotransducer channels may constitute a major cause of cochlear outer hair cell vulnerability and high-frequency hearing loss
physiological function
-
luteolin enhances sarcoplasmic reticulum Ca2+-ATPase activity to improve systolic/diastolic function during ischemia/reperfusion in rat hearts and cardiomyocytes by attenuating the inhibitive effects of the p38 pathway on phospholamban
physiological function
-
plasma membrane Ca2+-ATPase 1 is required for maintaining atrial Ca2+ homeostasis and electrophysiological stability in mouse atria under stress conditions
physiological function
-
plasma membrane Ca2+-ATPase 2 regulates breast cancer cell proliferation and sensitivity to doxorubicin
physiological function
-
the enzyme contributes to the migration of lymphoid chemokine CCL21-activated dendritic cells as an important feature of the adaptive immune response
physiological function
the enzyme maintains Ca2+ homeostasis in molting glands/Y-organs of Callinectes sapidus
physiological function
-
the enzyme mediates sperm chemotaxis towards sperm-activating and attracting factor
physiological function
-
the enzyme removes excess Ca2+ from the cytosol and maintains intracellular Ca homeostasis essential for the living cell
physiological function
artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress
physiological function
artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress. Wild-type cells exhibit a significant increase in ROS production following treatment with artemisinin. Enzyme Pmr1p may play a role in ROS generation or accumulation from artemisinin
physiological function
ECA1 is originally identified as Ca2+ transporter, but has subsequently been shown to also transport Mn2+. AtECA1 is an endoplasmic reticulum (ER) Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction. Mn2+ has a critical role in the water oxidation step of photosynthesis, and the chloroplast is the second-largest sink for Mn2+ in the cell
physiological function
enzymes Pmr1 and Pdt1 cooperatively regulate cell morphogenesis through the control of Mn2+ homeostasis, and calcineurin functions as a Mn2+ sensor as well as a Mn2+ homeostasis regulator. The pmr1+ gene has strong genetic interactions with pdt1+ gene that encodes the Nramp-related divalent metal transporte. Pmr1 is regulated by the Ca2+/calcineurin/Prz1 pathway
physiological function
PMR1 is a Golgi Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction
physiological function
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artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress
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physiological function
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the enzyme mediates sperm chemotaxis towards sperm-activating and attracting factor
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physiological function
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enzymes Pmr1 and Pdt1 cooperatively regulate cell morphogenesis through the control of Mn2+ homeostasis, and calcineurin functions as a Mn2+ sensor as well as a Mn2+ homeostasis regulator. The pmr1+ gene has strong genetic interactions with pdt1+ gene that encodes the Nramp-related divalent metal transporte. Pmr1 is regulated by the Ca2+/calcineurin/Prz1 pathway
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physiological function
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artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress. Wild-type cells exhibit a significant increase in ROS production following treatment with artemisinin. Enzyme Pmr1p may play a role in ROS generation or accumulation from artemisinin
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physiological function
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PMR1 is a Golgi Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.22). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction
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physiological function
Plasmodium falciparum isolate K1
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artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress
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additional information
a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
additional information
a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
additional information
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a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
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A56S
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the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
R123I
site-directed mutagenesis, when Arg123 of ShMTP1 is mutated to Ile, the ability to confer Mn tolerance to either yeast or Arabidopsis is completely lost
R59A
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the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
S19A
the mutant shows 95% of wild type activity
S19D
the mutant with 163% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S22A
the mutant shows 70% of wild type activity
S22D
the mutant with wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S27A
the mutant shows 127% of wild type activity
S27D
the mutant with 89% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus
S29A
the mutant shows 60% of wild type activity
S29D
the mutant shows 64% of wild type activity
S57A
the mutant shows 50% of wild type activity
S57D
the mutant with 120% of wild type activity is deregulated by showing low activation by calmodulin and tryptic cleavage of the N-terminus. The mutant shows 10fold higher affinity towards calmodulin compared to the wild type enzyme
S99A
the mutant shows 78% of wild type activity
S99D
the mutant with 77% of wild type activity shows half of the wild type affinity towards calmodulin
Y62A
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the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold
D351N
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a phosphorylation site mutant, catalytically inactive
E309Q
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the mutation of Ca2+-binding site II leads to non-cooperative binding of only one Ca2+, and loss of ATPase activation, catalytically inactive mutant
E771Q
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the mutation of Ca2+-binding site I leads to no Ca2+ binding to either site, catalytically inactive mutant
F1110A
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2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
I274V
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Darier disease causing, 64% activity in comparison to wild-type enzyme
L321F
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Darier disease causing mutant, the mutant has the dramatically reduced sensitivity to the feedback inhibition by the accumulated lumenal Ca2+, the insensitivity to luminal Ca2+ raises this ion to an abnormally elevated level, 100% activity in comparison to wild-type enzyme
M719I
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Darier disease causing, 69% activity in comparison to wild-type enzyme
R268Q
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the mutation in isoform PMCA4 is likely causative for autosomal dominant familial spastic paraplegia
V1107A
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2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
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
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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
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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
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displays about 30% reduced ATP turnover rate relative to wild type, whereas the ATP turnover rate is reduced by about 80%
I188F
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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
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the mutant displays around 40% Ca2+ transport, compared with its about 70% rate of ATP turnover relative to the wild type enzyme
K205A
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the molecular rate of Ca2+-activated ATP hydrolysis at 37°C with 5 mM MgATP slightly lower than that of wild type enzyme
K205E
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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
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the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme
K234G
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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
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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
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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
D100A
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
D136A
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
D100A
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site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
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D136A
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site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
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D354A
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the mutant enzyme is not getting phosphorylated
D366A
catalytically inactive
additional information
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the N-deleted mutant DELTA74-ACA8 is also activated by acidic phospholipids
additional information
recombinant ECA1 shows ability to confer tolerance to toxic concentrations of Mn when heterologously expressed in a Mn-sensitive mutant yeast strain. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrates a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants
additional information
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construction of a pmr1 knockout mutant, which shows high sensitivity to Mn2+ and EGTA, but also resistance to oxidative stress and suppression of highly reactive oxygen species sensitivity od smf3 RNA-mediated interference and daf16 worms, overview
additional information
disruption of gene PMR1 homologue CaPMR1 leads to inhibition of many Golgi-located, Mn2+-dependent mannosyltransferases, the Capmr1DELTA null mutant is viable in vitro and without phenotype on media supplemented with Ca2+ and Mn2+, but loose viability on minimal medium with low Ca2+/Mn2+ concentrations and enter in stationary phase, growth and glycosylation defects, overview
additional information
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disruption of gene PMR1 homologue CaPMR1 leads to inhibition of many Golgi-located, Mn2+-dependent mannosyltransferases, the Capmr1DELTA null mutant is viable in vitro and without phenotype on media supplemented with Ca2+ and Mn2+, but loose viability on minimal medium with low Ca2+/Mn2+ concentrations and enter in stationary phase, growth and glycosylation defects, overview
additional information
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2-chloro-(epsilon-amino-Lys75)-[6-(4-[N,N-diethylamino]phenyl)-1,3,5-triazin]-4-yl-calmodulin-labeled calmodulin is used for determination of enzyme amino acids essential for binding, peptide mapping with full-length binding site peptide 28 and truncated and mutated versions, overview
additional information
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construction of a pmr1 null mutant, the mutant strain exhibits growth defects in media with added EGTA, the defect is reversible by addition of Ca2+ or Mn2+, the latter with less effect
additional information
a splice variant PMCA4b-Asp mutant exhibits 10% of the Ca2+ efflux activity of wild type isoform PMCA4
additional information
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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
additional information
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DELTAPCA1 mutants fail to restore resting Ca2+ levels after salt stress treatments
additional information
Plasmodium falciparum mutant PfATP6DELTA phenotype, overview
additional information
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Plasmodium falciparum mutant PfATP6DELTA phenotype, overview
additional information
Plasmodium falciparum isolate K1
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Plasmodium falciparum mutant PfATP6DELTA phenotype, overview
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additional information
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Plasmodium falciparum mutant PfATP6DELTA phenotype, overview
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additional information
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the yeast strain K610, which has the pmr1DELTA mutation, has the highest sensitivity to CdCl2 at a final concentration of 0.02 mM
additional information
construction of a pmr1 knockout (DELTApmr1) cells exhibiting hypersensitivity to EGTA. Overexpression of pdt1+ gene suppresses the EGTA-sensitive growth defects of DELTApmr1 cells. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
additional information
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construction of a pmr1 knockout (DELTApmr1) cells exhibiting hypersensitivity to EGTA. Overexpression of pdt1+ gene suppresses the EGTA-sensitive growth defects of DELTApmr1 cells. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
additional information
Saccharomyces cerevisiae strain BY4742 cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast mutant pmr1DELTA phenotype, overview
additional information
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Saccharomyces cerevisiae strain BY4742 cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast mutant pmr1DELTA phenotype, overview
additional information
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construction of a pmr1 knockout (DELTApmr1) cells exhibiting hypersensitivity to EGTA. Overexpression of pdt1+ gene suppresses the EGTA-sensitive growth defects of DELTApmr1 cells. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
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additional information
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Saccharomyces cerevisiae strain BY4742 cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast mutant pmr1DELTA phenotype, overview
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