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Protease‐catalyzed peptide synthesis using inverse substrates: The influence of reaction conditions on the trypsin acyl transfer efficiency
Author(s) -
Schellenberger Volker,
Jakubke HansDieter,
Zapevalova Nina P.,
Mitin Yuri V.
Publication year - 1991
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260380114
Subject(s) - trypsin , protease , chemistry , catalysis , peptide , inverse , biochemistry , combinatorial chemistry , enzyme , stereochemistry , geometry , mathematics
Benzyloxycarbonyl‐ L ‐alanine p‐guanidinophenyl ester behaves as a trypsin “inverse substrate,” i.e., a cationic center is included in the leaving group instead of being in the acyl moiety. Using this substrate as an acyl donor, trypsin catalyzes the synthesis of peptide bonds that cannot be split by this enzyme. An optimal acyl transfer efficiency was achieved between pH 8 and 9 at 30°C.The addition of as much as 50% cosolvent was shown to be of minor influence on the acyl transfer efficiency, whereas the reaction velocity decreases by more than one order of magnitude. The efficiency of H‐Leu‐NH 2 and H‐Val‐NH 2 in deacylation is almost the same for “inverse” and normal type substrates.

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