ISSN:
1075-2617
Keywords:
α-chymotrypsin
;
enzymatic peptide synthesis
;
frozen system
;
Nα-unprotected substrates
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The ability of the endopeptidase α-chymotrypsin (EC 3.4.21.1) to catalyse the reaction of various Nα- unprotected di- and tripeptide ester derivatives with H-Leu-NH2, and with a series of C-terminal free di- and tripeptides at -15° C in frozen aqueous solution was investigated. The enzyme is able to synthesize N- and C-terminal unprotected penta- and hexapeptides in up to 92% yield, depending on the amino component used, in a single-step segment-condensation reaction. Freezing the reaction mixture resulted in significantly increased peptide yields compared with the reaction at room temperature. The enzyme shows a modified nucleophilic specificity in frozen solution compared with room temperature. Nucleophilic amino components with positively charged amino acids in P2′ -position are accepted. © 1997 European Peptide Society and John Wiley & Sons, Ltd.
Additional Material:
3 Ill.
Type of Medium:
Electronic Resource
