PMID: 2123861Dec 1, 1990Paper

Extracellular Ca2(+)-dependent inducible alkaline phosphatase from extremely halophilic archaebacterium Haloarcula marismortui

Journal of Bacteriology
S GoldmanM Mevarech

Abstract

When starved of inorganic phosphate, the extremely halophilic archaebacterium Haloarcula marismortui produces the enzyme alkaline phosphatase and secretes it to the medium. This inducible extracellular enzyme is a glycoprotein whose subunit molecular mass is 160 kDa, as estimated by sodium dodecyl sulfate-gel electrophoresis. The native form of the enzyme is heterogeneous and composed of multiple oligomeric forms. The enzymatic activity of the halophilic alkaline phosphatase is maximal at pH 8.5, and the enzyme is inhibited by phosphate. Unlike most alkaline phosphatases, the halobacterial enzyme requires Ca2+ and not Zn2+ ions for its activity. Both calcium ions (in the millimolar range) and NaCl (in the molar range) are required for the stability of the enzyme.

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Citations

Jul 1, 1992·Current Microbiology·T Karunakaran, P Gunasekaran
Nov 8, 2008·Protein Engineering, Design & Selection : PEDS·P G BagosS J Hamodrakas
Mar 7, 2014·Acta Crystallographica. Section D, Biological Crystallography·Shigeki AraiRyota Kuroki
Sep 26, 2001·Applied and Environmental Microbiology·S ZappaJ Dietrich
Sep 9, 2005·Microbiology and Molecular Biology Reviews : MMBR·Jerry Eichler, Michael W W Adams
Apr 27, 2002·Journal of Bacteriology·Brian H Lower, Peter J Kennelly
Oct 1, 1996·Applied and Environmental Microbiology·P de PradaJ E Brenchley
Mar 26, 2004·Journal of Inorganic Biochemistry·S ZappaE R Kantrowitz
Dec 9, 2021·Extremophiles : Life Under Extreme Conditions·Lorenzo CarréBruno Franzetti

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