Peptide synthesis by chymotrypsin in frozen solutions

FEBS Letters

Meos, Helle¹  Jakubke, Hans-Dieter³  Aaviksaar, Aavo²  Haga, Mati¹  Tõugu, Vello¹ 

[1] Laboratory of Bioorganic Chemistry, Institute of Chemical Physics and Biophysics, Akadeemia 23, Tallinn EE0026, Estonia;Institute of Experimental Biology, Harju Harku EE3051, Estonia;University of Leipzig, Biosciences Division, Department of Biochemistry, Talstr. 33, D-0-7010 Leipzig, Germany

关键词: α-Chymotrypsin;    Nucleophile specificity;    Frozen solution;    HPLC;    high performance liquid chromatography;    OEt;    ethyl ester;    OMe methyl ester;    Ac;    acetyl;    Mal;    maleyl;    Bz;    benzoyl;    Cit;    citrulline;    Orn;    ornithine;    X;    amino acid residue. Amino acids were of l-configuration;   

DOI  :  10.1016/0014-5793(93)80188-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown