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Conformation of the primary binding loop folded through an intramolecular interaction contributes to the strong chymotrypsin inhibitory activity of the chymotrypsin inhibitor from Erythrina variegata seeds


Conformation of the primary binding loop folded through an intramolecular interaction contributes to the strong chymotrypsin inhibitory activity of the chymotrypsin inhibitor from Erythrina variegata seeds



Journal of Biochemistry 126(1): 162-167



ISSN/ISBN: 0021-924X

PMID: 10393334

DOI: 10.1093/oxfordjournals.jbchem.a022417

Previous studies showed that the amino acid residues Gln62, Phe63, Leu64 and Phe67 in the primary binding loop of Erythrina variegata chymotrypsin inhibitor (ECI) are involved in its strong inhibitory activity towards chymotrypsin. The present study examined whether these 4 amino acid residues are predominantly involved in the strong inhibitory activity by simultaneous substitution of the residues by alanine.

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Accession: 003077465

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