The promiscuous phosphomonoestearase activity of Archaeoglobus fulgidus CopA, a thermophilic Cu+ transport ATPase
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- 作者：Luis M. Bredeston ; F. Luis Gonzá ; lez Flecha ; lgf@qb.ffyb.uba.ar" class="auth_mail" title="E-mail the corresponding author
- 关键词：Af-CopA ; Cu(I)-transport ATPase from Archaeglobus fulgidus ; DDM ; n-dodecyl β-D-maltoside ; DTT ; Dithiothreitol ; HAD ; Haloacid dehalogenase ; MOPS ; 3-(N-morpholino)propanesulfonic acid ; PC ; Phosphatidylcholine ; PE ; Phosphatidylethanolamine ; Pi ; Inorganic phosphate ; XPL ; Phospholipid mole fraction in the micellar phase ; PMCA ; Plasma membrane Ca2 ; +-ATPase ; PNPP ; p-nitrophenyl phosphate ; PS ; Phosphatidylserine ; SERCA ; Sarcoplasmic reticulum Ca2 ; +-ATPase ; TM-MBSs ; Transmembrane metal binding
- 刊名：Biochimica et Biophysica Acta (BBA)-Biomembranes
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：1858
- 期：7
- 页码：1471-1478
- 全文大小：576 K
文摘
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The promiscuous phosphomonoestearase activity of Af-CopA is characterized and compared with the principal ATPase activity.
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The enzyme is more efficient for capturing ATP, but pNPP would be better placed at the catalytic site.
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Both activities are enhanced by Mg2 + (essential) and phospholipids (non-essential),
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Salts and Cu+ have opposite effects on the ATPase and phosphatase activities.
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Catalysis of both substrates is driven by an enthalpy lowering mechanism.