Nosaka K, Kaneko Y, Nishimura H, Iwashima A
Department of Biochemistry, Kyoto Prefectural University of Medicine, Japan.
FEMS Microbiol Lett. 1989 Jul 1;51(1):55-9. doi: 10.1016/0378-1097(89)90077-3.
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.
通过遗传分析证明,酿酒酵母中的周质可溶性硫胺素结合蛋白(岩岛,A.等人(1979年)《生物化学与生物物理学报》577,217 - 220)由编码硫胺素可阻遏酸性磷酸酶的PHO3基因编码(施温格鲁伯,M.E.等人(1986年)《生物化学杂志》261,15877 - 15882)。与亲代细胞相比,酿酒酵母的pho3突变细胞对[14C]硫胺素磷酸盐的摄取活性显著降低,这表明硫胺素可阻遏酸性磷酸酶在酿酒酵母摄取硫胺素部分之前,在周质空间中硫胺素磷酸盐的水解过程中发挥作用。