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Truncated reactive center loop decrease the inhibitory activity of Antheraea pernyi serine protease inhibitor 6
Author(s) -
Wang Guobao,
Na Shuang,
Qin Li
Publication year - 2020
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21727
Subject(s) - antheraea pernyi , prophenoloxidase , serine protease , biology , serine , amino acid , recombinant dna , biochemistry , mutagenesis , inhibitory postsynaptic potential , active center , protease , microbiology and biotechnology , mutation , enzyme , receptor , gene , neuroscience , innate immune system
Abstract Here, we assessed the effect of a systematic change in reactive center loop (RCL) length, N‐terminal to the reactive center, on the inhibitory activity of the recombinant Apserpin‐6. The domain prediction results indicated that the RCL is located between the amino acid numbered 359–379 at the C‐terminal of Apserpin‐6. The N‐terminal variable region for amino acid positions P7–P1 of the RCL of Apserpin‐6 was truncated or extended by residue deletion or insertion using site‐directed mutagenesis. The recombinant Apserpin‐6 with one or two residues insertion in RCL had no effect on prophenoloxidase (proPO) activity, whereas deletion of one or two residues in RCL lowered the efficiency of inhibition of Apserpin‐6. The results of this study will facilitate the understanding of inhibition mechanism of RCL on proPO activity.