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Alpha-chymotrypsin-catalyzed peptide synthesis using N-protected D-amino acid carbamoylmethyl esters as acyl donors.

作者信息

Salam Sayed Mohiuddin Abdus, Kagawa Ken-Ichi, Kawashiro Katsuhiro

机构信息

Department of Chemical Science and Technology, Faculty of Engineering, The University of Tokushima, 770-8506, Minamijosanjima, Tokushima, Japan.

出版信息

Biotechnol Lett. 2005 Aug;27(16):1199-203. doi: 10.1007/s10529-005-0018-8.

DOI:10.1007/s10529-005-0018-8
PMID:16158264
Abstract

Alpha-chymotrypsin-catalyzed peptide synthesis was carried out between an N-protected D-amino acid ester and an L-amino acid amide (acyl donor, 10 mM; acyl acceptor, 50 mM; enzyme, 2 mg ml(-1); pH 8). By using a highly reactive carbamoylmethyl (Cam) ester as acyl donor, the D-amino acid was incorporated into the N-terminus of the resulting dipeptide amide. N-Protected dipeptide amides bearing D-amino acids such as D-Phe, D-Leu and D-Ala at their N-terminus were synthesized in high yields (up to 80%) in 1-3 h.

摘要

相似文献

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Alpha-chymotrypsin-catalyzed peptide synthesis using N-protected D-amino acid carbamoylmethyl esters as acyl donors.
Biotechnol Lett. 2005 Aug;27(16):1199-203. doi: 10.1007/s10529-005-0018-8.
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