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EC Number	Posttranslational Modification	Commentary	Reference
3.4.21.83	proteolytic modification	treatment of enzyme PSP with immobilized trypsin (immobilized on modified porous glass) leads to production of a stable truncated enzyme form (PSP-Tr with about 75 kDa) which lacks 22 C-terminal amino acid residues and completely loses enzymatic activity, presumably because of changes in the nearest environment of His652 of the catalytic triad. The truncated enzyme, i.e. PSP-Chtr, prepared via cleavage with immobilized chymotrypsin (immobilized on modified porous glass) lacks the N-terminal region of the molecule that envelops the catalytic domain of PSP and supposedly prevents hydrolysis of high molecular weight substrates. The lacking fragment corresponds to the N-terminal highest rank element of the informational structure of PSP	-, 752738

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Release 2023.1 (January 2023)