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. 1989 Jul 1;51(1):55-9.
doi: 10.1016/0378-1097(89)90077-3.

A possible role for acid phosphatase with thiamin-binding activity encoded by PHO3 in yeast

K Nosaka  1 , Y Kaneko, H Nishimura, A Iwashima
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A possible role for acid phosphatase with thiamin-binding activity encoded by PHO3 in yeast

K Nosaka et al. FEMS Microbiol Lett. .

Abstract

Periplasmic soluble thiamin-binding protein in Saccharomyces cerevisiae (Iwashima, A. et al. (1979) Biochim. Biophys. Acta 577, 217-220) was demonstrated to be encoded by PHO3 gene that codes for thiamin repressible acid phosphatase (Schweingruber, M.E. et al. (1986) J. Biol. Chem. 261, 15877-15882) by genetic analysis. The pho3 mutant cells of S. cerevisiae in contrast to the parent cells have markedly reduced activity of the uptake of [14C]thiamin phosphates, suggesting that thiamin repressible acid phosphatase plays a role in the hydrolysis of thiamin phosphates in the periplasmic space prior to the uptake of their thiamin moieties by S. cerevisiae.

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