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Peptide synthesis by chymotrypsin in frozen solutions
Author(s) -
Tõugu Vello,
Meos Helle,
Haga Mati,
Aaviksaar Aavo,
Jakubke Hans-Dieter
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80188-z
Subject(s) - chemistry , tyrosine , peptide , chymotrypsin , amino acid , stereochemistry , peptide synthesis , nucleophile , catalysis , biochemistry , enzyme , trypsin
Nucleophilic efficiency of free amino acids in chymotrypsin‐catalyzed acyl transfer in ice at −18°C using ethyl esters of N ‐maleyl‐ l ‐tyrosine and l ‐tyrosine as the acyl group donors has been studied. Although the amino acids did not act as acyl acceptors in liquid water, the high yields of peptides were obtained in frozen solutions at pH 10.5 (before freezing). The efficiency of amino acids in the formation of the corresponding dipeptides depended on the substrate used, and decreased in the order Ser,Thr,Gln>Lys>Cit>Ala>Gly>Asn>Arg>Glu>Val>Orn>Asp (with no peptide formed with His, Leu, He and Pro) for N ‐maleyl‐ l ‐tyrosine ethyl ester and Ser>Lys>Orn>Arg,Cit>Gln>Thr>Asn>Ala>Gly (with no peptide formed with Glu, Val, Asp, His, Leu, Ile and Pro) for l ‐tyrosine ethyl ester.