Peptide synthesis by chymotrypsin in frozen solutions

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...

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Bibliographic Details
Published inFEBS letters Vol. 329; no. 1-2; pp. 40 - 42
Main Authors Tõugu, Vello, Meos, Helle, Haga, Mati, Aaviksaar, Aavo, Jakubke, Hans-Dieter
Format Journal Article
LanguageEnglish
Published 23.08.1993
Subjects
Ac, acetyl
Bz, benzoyl
Cit, citrulline
Frozen solution
HPLC, high performance liquid chromatography
Mal, maleyl
Nucleophile specificity
OEt, ethyl ester
OMe methyl ester
Orn, ornithine
X, amino acid residue. Amino acids were of l-configuration
α-Chymotrypsin
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)80188-Z