Structure and Function of a Pepstatin-Insensitive Acid Proteinase from Aspergillus Niger var. Macrosporus

Kenji Takahashi,Masaki Kojima,Takao Kimura,Osamu Makabe,Toshio Takizawa,Masaru Tanokura,Toru Hamaya,Hideshi Inoue,Yutaka Muto,Eiichiro Suzuki,Hiroshi Miyano,Makoto Yamasaki

doi:10.1007/978-1-4684-6012-4_24

Kenji Takahashi, Masaki Kojima + Show 10 more

https://doi.org/10.1007/978-1-4684-6012-4_24

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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.KeywordsCircular DichroismAspergillus NigerCircular Dichroism SpectrumAspartic ProteinaseAcid ProteinaseThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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