Abstract
Achromobacter protease I (API) is an extracellular protease isolated from Achromobacter lyticus M497-1 (Masaki et al., 1978) and is specific to lysyl bonds including Lys-Pro bond. In addition, API has several attractive properties (Masaki et al., 1981a; Masaki et al., 1981b): (i) Its proteolytic activity is an order of magnitude higher than that of bovine trypsin, (ii) It has a broad pH optimum ranging from 8.5–10.7, (iii) It exhibits full activity in the presence of 5 M urea or 0.1% SDS. Accordingly, API has been widely used as a tool for the primary fragmentation of polypeptide in protein sequence analysis. In this paper, we describe the structural basis of the specificity for lysine and compare it with that of bovine trypsin.
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© 1993 Springer Science+Business Media New York
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Norioka, S., Sakiyama, F. (1993). Lysine-Specific Serine Protease from Achromobacter Lyticus: Its Substrate Specificity and Comparison with Trypsin. In: Imahori, K., Sakiyama, F. (eds) Methods in Protein Sequence Analysis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1603-7_13
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DOI: https://doi.org/10.1007/978-1-4899-1603-7_13
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