PMID: 208203Mar 1, 1978Paper

Inhibition of alkaline phosphatase I of Pichia guilliermondii yeast in vitro and in vivo

Ukrainskiĭ biokhimicheskiĭ zhurnal
A A Sibirnyi, G M Shavlovskiĭ

Abstract

The rate of p-nitrophenyl phosphate and flavin mononucleotide (FMN) hydrolysis by the partially purified preparation of alkaline phosphatase I of Pichia guilliermondii flavinogenic yeast was studied as affected by different substrates and inorganic ions. Their Km was established to be 2.0 X 10(-4) m and 2.5 X 10(-4) M, respectively. Dephosphorylation of p-nitrophenylphosphate and FMN was inhibited competitively by beta-glycerophosphate (Ki = 3.1 X 10(-3) M, respectively). The presence of inorganic phosphate ions in the reaction mixture decreases or removes inhibition of these compounds hydrolysis by other substrates of alkaline phosphatase I. The activity of alkaline phosphatase I increases in the presence of Mg2+ and was strongly inhibited in the presence of Be2+, Cu2+, Zn2+, Cd2+ and inorganic phosphate, the mixture of Be2+ and F- being the most effective. This mixture inhibited the phosphatase activity of the partially purified preparation of alkaline phosphatase I of the cell-free extract as well as of intact cells in both the alkaline and acid zones of pH (8.6 and 5.5, respectively). Incubation of the washed iron-deficient P. guilliermondii cells in the presence of Be2+ and F- did not result in accumulation of FMN in the y...Continue Reading

Related Concepts

Alkaline Phosphatase
Cochliobolus
Beryllium
Cations, Divalent
Fluorides
Flavin Mononucleotide Monosodium Salt, Dihydrate
Calcium Glycerophosphate
Nitrophenyl Phosphatase
Orthophosphate
Pichia

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