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

S. Goldman, K. Hecht, H. Eisenberg, M. Mevarech*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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 require 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.

Original languageEnglish
Pages (from-to)7065-7070
Number of pages6
JournalJournal of Bacteriology
Volume172
Issue number12
DOIs
StatePublished - 1990

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