126693-47-8Relevant articles and documents
Resolution of non-proteinogenic amino acids via microbial lipase-catalyzed enantioselective transesterification
Miyazawa, Toshifumi,Mio, Motoe,Watanabe, Yuko,Yamada, Takashi
, p. 219 - 224 (2008/09/20)
A number of non-proteinogenic amino acids bearing aliphatic side chains were resolved with moderate to good enantioselectivities (E = 15-42) through the Burkholderia cepacia lipase-catalyzed enantioselective transesterification of the 2,2,2-trifluoroethyl esters of their N-benzyloxycarbonyl derivatives with methanol as a nucleophile in diisopropyl ether.
α-chymotrypsin-catalysed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in organic solvents with low water content: Incorporation of non-protein amino acids into peptides
Miyazawa, Toshifumi,Nakajo, Shin'ichi,Nishikawa, Miyako,Hamahara, Kazumi,Imagawa, Kiwamu,Ensatsu, Eiichi,Yanagihara, Ryoji,Yamada, Takashi
, p. 82 - 86 (2007/10/03)
The α-chymotrypsin-catalyzed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in orgnanic solvents with low water content was presented. The methyl esters of N-Z derivatives of racemic non-protein amino acids were chosen as carboxy components. They allowed the peptide-bond formation and optical resolution simultaneously to yield homochiral peptides. This method is useful for the incorporation of non-protein amino acids into peptides.
Porcine Pancreatic Lipase Catalyzed Enantioselective Hydrolysis of Esters of N-Protected Unusual Amino Acids
Miyazawa, Toshifumi,Iwanaga, Hitoshi,Ueji, Shinichi,Yamada,Takashi,Kuwata, Shigeru
, p. 2219 - 2222 (2007/10/02)
Porcine pancreatic lipase catalyzed the highly enantioselective hydrolysis of a kind of α-substituted carboxylic esters, i.e., the 2,2,2-trifluoroethyl esters of the N-benzyloxycarbonyl derivatives of unusual amino acids.
