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Could domain movements be involved in the mechanism of trypsin‐like serine proteases?
Author(s) -
Dufton M.J.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80360-u
Subject(s) - proteases , mechanism (biology) , serine , trypsin , chemistry , domain (mathematical analysis) , microbiology and biotechnology , biochemistry , biophysics , enzyme , biology , philosophy , mathematical analysis , mathematics , epistemology
It is hypothesised that the characteristic twin domain structure of serine proteases permits important allosteric responses in the molecule when peptide and protein substrates bind. Such movement would be ideal for stressing the scissile bond in the substrate, thereby making the task of hydrolysis substantially easier. The control of the domain movement can be closely associated with substrate binding, via the N‐ and C‐terminal regions of the enzyme. The hypothesis also suggests that certain inhibitory peptides exert their effect by binding without inducing the domain movement.