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. 1976 Jul 1;157(1):161-7.
doi: 10.1042/bj1570161.

Isolation and properties of a small manganese-ion-stimulated bacterial alkaline phosphatase

P S Fitt, P I Peterkin

Isolation and properties of a small manganese-ion-stimulated bacterial alkaline phosphatase

P S Fitt et al. Biochem J. .

Abstract

1. An alkaline phosphatase was partially purified from extracts of Halobacterium cutirubrum. 2. The enzyme has a mol.wt. of 15 500 and is therefore less than one-quarter of the size of other known bacterial alkaline phosphatases. 3. It is stimulated up to ten-fold by Mn2+, but not by Ca2+ or Mg2+. 4. The activities with and without Mn2+ cannot be separated by gel filtration and have similar restricted substrate specificities. 5. The only substrates for the enzyme that have so far been found are p-nitrophenyl phosphate, 5'-dATP, 5'-dTMP and 5'-dTTP.

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