Enzymatic approach to both enantiomers of N-Boc hydrophobic amino acids

Enzymatic approach to both enantiomers of N-Boc hydrophobic amino acids
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DOI:
10.1016/j.tetasy.2006.07.012
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发表时间:
2006-08-14
影响因子:
--
通讯作者:
Canevotti, Renato
Canevotti, Renato
中科院分区:
其他
文献类型:
--
作者:
Agosta, Eleonora;Caligiuri, Antonio;Canevotti, Renato

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蛋白酶催化N-BOC氨基酸酯的水解使我们能够在优质ee中获得N-BOC氨基酸丁酸、去亮氨酸、去缬氨酸、亮氨酸和t-亮氨酸的l -酸和d -酯。反应时间短,反应浓度高。当采用双相体系(缓冲液- mtbe)时,观察到很强的溶剂效应。该方法对d -t-亮氨酸的制备具有重要意义,目前尚无实用的制备方法。(c) 2006 Elsevier Ltd.版权所有。
Protease catalysed hydrolysis of N-Boc-amino acid esters allows us to obtain N-BOC L-acids and D-esters of amino butanoic acid, nor-leucine, nor-valine, leucine and t-leucine in excellent ee. The reaction occurs in short reaction times and high concentrations. When a biphasic system (buffer-MTBE) is employed, a strong solvent effect is observed. This method could be of significance for the preparation of D-t-leucine, for which a practical method is currently unavailable. (c) 2006 Elsevier Ltd. All rights reserved.