Acid phosphatase Saccharomyces

A repressible acid phosphatase of Saccharomyces mellis develops when the organism is grown in a medium free of phosphate. Only traces of enzymic activity are found when media containing inorganic phosphate are used. The enzyme is inhibited by phosphate, arsenate, molybdate, and borate (117). 

Bergman, L.W., McClinton, D.C., Madden, S.L. Preis, L.H. (1986). Molecular analysis of the DNA sequences involved in the transcriptional regulation of the phosphate-repressible acid phosphatase gene (PH05) of Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences (USA) 83, 6070-4. 

K. A. Bostian, J. M. Lemize and H. O. Halvorson (1983). Physiological control of repressible acid phosphatase gene transcripts in Saccharomyces cerevisiae. Mol. Cell Biol., 3, 839-853. 

R. Weimberg and W. L. Orton (1964). Evidence for an exocellular site for the acid phosphatase of Saccharomyces mellis. J. Bacteriol., 88, 1743-1152. 

The extracellular enzymes of yeast are glycoproteins and include invertase and acid phosphatase. Strains of Saccharomyces carlsbergensis but not S, cerevisiae also possess melibiase. Yeast invertase has a minimum molecular weight of 27 000 contains 50 % mannan and 2-3 % glucosamine [43]. The precise location of the extracellular enzymes is still uncertain. They may occupy the space (periplasm) between the membrane and the bulk of the wall components, be anchored to the membrane via protein or covalently associated with other mannan or even glucan molecules. 

Some of the l,3-dihydroxy-2-propanone phosphate (see Fig. 4) may be reduced to glycerol 3-phosphate, which is then hydrolyzed by a specific phosphatase to glycerol, and this is eliminated from the cells.243 Certain yeasts are notorious for producing acid Saccharomyces bailii (Zygosaccharomyces acidifaciens)... 

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