The 40 kDa secreted aspartyl proteinase (Sapt1) of is a pepsin-like enzyme encoded by the gene. According to the deduced amino acid sequence, Sapt1 has a putative preproregion of 60 amino acids preceding the mature enzyme. Maturation and processing of Sapt1 was analysed in and strains expressing wild-type or mutated forms of In the glycosylated 46 kDa proenzyme was converted to the mature 40 kDa form of Sapt1 by -dependent proteolytic cleavage following the Lys-Arg sequence. The replacement of Lys-Arg by Lys-Gly revealed that the precursor can be processed by an autocatalytic cleavage. This alternative processing pathway to produce mature Sapt1 is less efficient than the Kex2-mediated pathway. Finally, it was shown that in and the removal of the proregion was a prerequisite for the secretion of Sapt1.


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