Abstract
Aspartic proteinase production is widespread among the fungi and examples of both secretion and localization in subcellular organelles are known. For example, the yeast Saccharomyces cerevisiae produces aspartic proteinases which reside in the vacuole (proteinase A, analagous to mammalian cathepsin D, Ammerer et al., 1986; Woolford et al., 1986) and within the secretory apparatus (product of the YAP3 gene, Egel-Mitani et al., 1990). It is likely that other fungi produce equivalent proteinases. In addition, yeasts secrete aspartic proteinases such as the barrier proteinase of S. cerevisiae (MacKay et al., 1988; this volume) and the PEPI proteinase of Saccharomycopsis fibuligera (Hirata et al., 1988). The genes for all these proteinases have been cloned and DNA sequences determined from which the amino acid sequences have been derived. Many filamentous fungi are also known to secrete aspartic proteinases and these, as well as secretion of heterologous aspartic proteinase by these fungi, will be the major focus of this chapter.
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Ward, M., Kodama, K.H. (1991). Introduction to Fungal Proteinases and Expression in Fungal Systems. In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_20
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DOI: https://doi.org/10.1007/978-1-4684-6012-4_20
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