The specificity of alkaline mesentericopeptidase (a proteinase closely related to subtilisin BPN') for the C-terminal moiety of the peptide substrate (Pi' specificity) has been studied in both hydrolysis and aminolysis reactions. N-Anthraniloylated peptide p-nitroanilides as fluorogenic substrates and amino acid or peptide derivatives as nucleophiles were used in the enzymic peptide hydrolysis and synthesis. Both hydrolysis and aminolysis kinetic data suggest a stringent specificity of mesentericopeptidase and related subtilisins to glycine as P1′ residue and predilection for bulky hydrophobic P2′ residues. A synergism in the action of S1′ and S2′subsites has been observed. It appears that glycine flanked on both sides by hydrophobic bulky amino acid residues is the minimal amino acid sequence for an effective subtilisin catalysis.
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December 1987
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Research Article|
December 15 1987
Glycine flanked by hydrophobic bulky amino acid residues as minimal sequence for effective subtilisin catalysis
E K Bratovanova;
E K Bratovanova
Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, 1040 Sofia, Bulgaria
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D D Petkov
D D Petkov
Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, 1040 Sofia, Bulgaria
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1987 London: The Biochemical Society
1987
Biochem J (1987) 248 (3): 957–960.
Citation
E K Bratovanova, D D Petkov; Glycine flanked by hydrophobic bulky amino acid residues as minimal sequence for effective subtilisin catalysis. Biochem J 15 December 1987; 248 (3): 957–960. doi: https://doi.org/10.1042/bj2480957
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