The Enzyme Database

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Accepted name: P-type Ca2+ transporter
Reaction: ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
Other name(s): sarcoplasmic reticulum ATPase; sarco(endo)plasmic reticulum Ca2+-ATPase; calcium pump; Ca2+-pumping ATPase; plasma membrane Ca-ATPase; Ca2+-transporting ATPaseP-
Systematic name: ATP phosphohydrolase (P-type, Ca2+-transporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
1.  Schatzmann, H.J. and Vicenzi, F.F. Calcium movements across the membrane of human red cells. J. Physiol. 201 (1969) 369–395. [DOI] [PMID: 4238381]
2.  Inesi, G., Watanabe, T., Coan, C. and Murphy, A. The mechanism of sarcoplasmic reticulum ATPase. Ann. N.Y. Acad. Sci. 402 (1982) 515–532. [DOI] [PMID: 6301340]
3.  Carafoli, E. The Ca2+ pump of the plasma membrane. J. Biol. Chem. 267 (1992) 2115–2118. [PMID: 1310307]
4.  MacLennan, D.H., Rice, W.J. and Green, N.M. The mechanism of Ca2+ transport by sarco(endo)plasmic reticulum Ca2+-ATPases. J. Biol. Chem. 272 (1997) 28815–28818. [DOI] [PMID: 9360942]
5.  Toyoshima, C., Nakasako, M., Nomura, H. and Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 (2000) 647–655. [DOI] [PMID: 10864315]
6.  Andersen, J.L., Gourdon, P., Moller, J.V., Morth, J.P. and Nissen, P. Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 718–722. [PMID: 21636921]
[EC created 1984 as as EC, transferred 2000 to EC, modified 2001, modified 2011, transferred 2018 to EC]

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