Isolation and properties of a small manganese-ion-stimulated bacterial alkaline phosphatase.
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.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000302:isolation & purification*; D003035:Cobalt / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D006217:Halobacterium / Q000201:enzymology*; D006358:Hot Temperature; D008345:Manganese / Q000494:pharmacology*; D008970:Molecular Weight; D009596:Nitrophenols / Q000378:metabolism; D009994:Osmolar Concentration; D012965:Sodium Chloride / Q000494:pharmacology; D013942:Thymine Nucleotides / Q000378:metabolism; D015032:Zinc / Q000494:pharmacology
D009596:Nitrophenols; D013942:Thymine Nucleotides; D003035:Cobalt; D008345:Manganese; D012965:Sodium Chloride; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D000469:Alkaline Phosphatase; D015032:Zinc