Abstract
As reported previously [1, 2], we succeeded in isolating Scytalidium lignicolum in 1972 [3], which produced S-PI (Pepstatin Ac) [4]-insensitive carboxyl proteinases. This strain produced four distinct carboxyl proteinases: A-1, A-2, B, and C [5–7]. None of them were inactivated by S-PI, diazoacetyl-DL-norleucinemethylester (DAN) [8], and 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP) [9]. However, as an exception, the carboxyl proteinase B was inactivated by EPNP. They had unique substrate specificities [10–14] in addition to a unique behavior against inhibitors. The complete amino acid sequence of carboxyl proteinase B [15] was quite different from those of other enzymes. Furthermore, it was found that unlike other carboxyl proteinases, one of the catalytic residues of the enzyme is glutamic acid [16, 17]. To our knowledge, it was the first demonstration of a glutamic proteinase. We have further demonstrated that enzymes having properties similar to those of Scytalidium were widely distributed among fungi [18–22], bacteria [23, 24] and thermophilic bacteria [25]. On the basis of the results obtained so far, we proposed that carboxyl proteinases should be classified into two groups: pepstatin-sensitive carboxyl proteinases (aspartic proteinase) and pepstatin-insensitive carboxyl proteinases (Scytalidium type) [1, 2].
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References
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K. Oda, et al., in preparation.
K. Oda, et al., in preparation.
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Oda, K., Takahashi, S., Shin, T., Murao, S. (1995). Pepstatin-Insensitive Carboxyl Proteinases. 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_69
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