Abstract
In addition to the extensively studied pepsin type aspartic proteinases, there exists a distinct family of acid proteinases that differ widely in both functional and structural aspects. Functionally, they are insensitive to more than one of the specific inhibitors for the pepsin type aspartic proteinases; i.e., pepstatin, l,2-epoxy-3-(p-nitrophenoxy)propane and diazoacetyl-DL-norleucine methyl ester. Structurally, no homology is observed in the primary structures, even in the Asp-Thr/Ser-Gly sequence that is conserved in the active sites of the aspartic proteinases. Because of these fundamental differences, this family is discriminated by the name, “non-pepsin type acid proteinase”.
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Kagami, N., Inoue, H., Kimura, T., Makabe, O., Takahashi, K. (1995). Expression in E.Coli of Aspergillus Niger Var. Macrosporus Proteinase A, a Non-Pepsin Type Acid Proteinase. In: Takahashi, K. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 362. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1871-6_80
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DOI: https://doi.org/10.1007/978-1-4615-1871-6_80
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