Two Alkaline Phosphatases from a Butirosin A Producer Bacillus vitellinus

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In low-phosphate medium, a butirosin A producer B. vitellinus produced two alkaline phosphatases. These enzymes were fractionated by DEAE-cellulose column chromatography. One phosphatase (Pho I) was eluted with the lower concentration of NaCl compared with the other phosphatase (Pho II). In the wild type strain, Pho I was completely repressed in the high-phosphate medium, but 30% of the fully-derepressed level of Pho II was still produced. The phosphatase-negative mutant, P-15, that was shown to accumulate butirosin A-6-N-diphosphate in our previous study, produced only one phosphatase (Pho I) under the low-phosphate condition. Therefore, P-15 was characteristic of the deficiency in Pho II synthesis. The partially purified preparations of Pho I and II were characterized. Although both enzymes had a similar molecular weight, they could be differentiated in control of synthesis, heat stability, substrate specificity and other properties. Kinetic properties showed that Pho-II was more specific than Pho I to aminoglycoside-phosphates; butirosin A-3-phosphate, butirosin A-6-N-diphosphate and 6-deamino-6-hydroxybutirosin A-6-O-diphosphate. The roles of the two phosphatases in butirosin A biosynthesis were discussed.
社団法人日本農芸化学会の論文