Literature DB >> 6804434

Monomeric alkaline phosphatase of Vibrio cholerae.

N K Roy, R K Ghosh, J Das.   

Abstract

Alkaline phosphatase has been purified to homogeneity from two strains of Vibrio cholerae. The enzymes from both strains are single polypeptides of molecular weight 60,000. Both of the enzymes have pH optima around 8.0 and can act on a variety of organic phosphate esters, glucose-1-phosphate being the best substrate. The enzymes are unable to hydrolyze ATP and AMP. Although they have identical Km values, the two enzymes differ significantly in Vmax with p-nitrophenyl phosphate as substrate. The enzymes from the two strains also differ in their sensitivity to EDTA, Pi, and metal ions and activities of the apoenzymes. Ca2+ reactivated the apoenzymes most.

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Year:  1982        PMID： 6804434      PMCID： PMC216319          DOI： 10.1128/jb.150.3.1033-1039.1982

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  14 in total

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