Premium
Chain Elongation of Thiodipeptides with Proteases
Author(s) -
Unverzagt Carlo,
Geyer Armin,
Kessler Horst
Publication year - 1992
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199212291
Subject(s) - proteases , elongation , racemization , chemistry , oligopeptide , chain (unit) , thioamide , stereochemistry , biochemistry , peptide , enzyme , materials science , ultimate tensile strength , physics , astronomy , metallurgy
The C‐terminal elongation of thiopeptides 1 is not possible by chemical activation—thiazolones 2 are the major products. Now with proteases as catalysts, 1 has been converted without racemization into oligopeptides 3 with thioamide groups in defined positions. All = allyl.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom