Dynamic kinetic resolution of amino acid amide catalyzed by D-aminopeptidase and α-amino-ε-caprolactam racemase

被引:49
作者
Asano, Y [1 ]
Yamaguchi, S [1 ]
机构
[1] Toyama Prefectural Univ, Biotechnol Res Ctr, Toyama 9390398, Japan
关键词
D O I
10.1021/ja050300m
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Amino acid amide racemizing activity was discovered in α-amino-ε-caprolactam (ACL) racemase (EC 5. 1. 1. 15) from Achromobacter obae. The enzymatic synthesis of d-alanine from l-alanine amide has been demonstrated by use of d-aminopeptidase (DAP; EC 3. 4. 11. 19) from Ochrobactrum anthropi C1-38 and ACL racemase. The conversion of 45 mM l-alanine amide was carried out at 30 °C for 7 h; l-alanine amide was completely converted to d-alanine, and no l-alanine was detected. The result of successive enzymatic reaction shows that the combination of ACL racemase and DAP can be applied for dynamic kinetic resolution of dl-amino acid amides to yield d-amino acids. Copyright © 2005 American Chemical Society.
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页码:7696 / 7697
页数:2
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