Abstract
The fungus Aspergillus niger var. macrosporus produces two extracellular acid proteinases, proteinases A and B.1–3 The acid proteinase B (Mr about 35 kDa) is sensitive to pepstatin, diazoacetyl-DL-norleucine methyl ester (DAN) and l,2-epoxy-3-(p-nitrophenoxy)propane (EPNP) and thus belongs to the ordinary aspartic proteinase family.4 On the other hand, the proteinase A (Mr about 22 kDa) is insensitive to pepstatin and also almost insensitive to DAN and EPNP,4 and shows substrate specificity fairly different from that of pepsin-type aspartic proteinases.5,6 These results indicate that the proteinase A belongs to a different acid proteinase family. This proteinase, therefore, seems to be an interesting object to investigate its structure/function relationships. Further, the study will contribute to a deeper understanding of the structure and function of the aspartic or acid proteinases in general.
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© 1991 Plenum Press, New York
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Takahashi, K. et al. (1991). Structure and Function of a Pepstatin-Insensitive Acid Proteinase from Aspergillus Niger var. Macrosporus . 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_24
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DOI: https://doi.org/10.1007/978-1-4684-6012-4_24
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