Peptide synthesis using carbamoylmethyl esters as acyl donors mediated by Bacillus amyloliquefaciens protease.
Bacillus amyloliquefaciens protease-catalyzed peptide bond formation was investigated using the carbamoylmethyl (Cam) ester as the acyl donor. A series of N-protected L-amino acid Cam esters were coupled with an L-amino acid amide in acetonitrile in good to excellent yields. The superiority of the Cam ester for segment condensations was demonstrated in several 2+1 couplings. Furthermore, the couplings of racemic amino acid Cam esters as carboxyl components afforded the L-L-peptides in a highly diastereoselective manner.
Miyazawa
Toshifumi
T
Department of Chemistry, Faculty of Science and Engineering, Konan University, Kobe 658-8501, Japan. miyazawa@konan-u.ac.jp
Shindo
Tadamichi
T
Murashima
Takashi
T
Yamada
Takashi
T
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology* / Q000378:metabolism; D055162:Biocatalysis; D004952:Esters / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D010452:Peptide Biosynthesis; D010447:Peptide Hydrolases / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry
D004952:Esters; D010455:Peptides; D010447:Peptide Hydrolases