Samenvatting
We describe a novel, organic cosolvent-stable and cation-independent engineered enzyme for peptide coupling reactions. The enzyme is a variant of a stable calcium-independent mutant of subtilisin BPN, with the catalytic Ser212 mutated to Cys and Pro216 converted to Ala. The enzyme, called peptiligase, catalyzes exceptionally efficient peptide coupling in water with a surprisingly high synthesis over hydrolysis (S/H) ratio. The S/H ratio of the peptide ligation reaction is correlated to the length of the peptide substrate and proved to be >100 for the synthesis of a 13-mer peptide, which corresponds to >99% conversion to the ligated peptide product and
Originele taal-2 | English |
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Pagina's (van-tot) | 2140-2147 |
Aantal pagina's | 8 |
Tijdschrift | Advanced Synthesis & Catalysis |
Volume | 358 |
Nummer van het tijdschrift | 13 |
DOI's | |
Status | Published - 30-jun.-2016 |