Enzyme promiscuity in earthworm serine protease: substrate versatility and therapeutic potential
Author:
Publisher
Springer Science and Business Media LLC
Subject
Organic Chemistry,Clinical Biochemistry,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s00726-015-2162-3.pdf
Reference79 articles.
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2. Banerjee R (2014) Introduction to the thematic minireview series on enzyme evolution. J Biol Chem 289(44):30196–30197
3. Bilej M, Brys L, Beschin A et al (1995) Identification of a cytolytic protein in the coelomic fluid of Eisenia fetida earthworm. Immunol Lett 45:123–128
4. Bilej M, Prochazkova P et al (2010) Invertebrate immunity. Adv Exp Med Biol 708:66–79
5. Boehlein SK, Rosa-Rodriguez JG et al (1997) Catalytic activity of the N-terminal domain of Escherichia coli asparagine synthetase B can be reengineered by a single-point mutation. J Am Chem Soc 119:5785–5791
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