|
type |
Journal Article |
authors |
Asano Y, Yamaguchi S. |
title |
Discovery of amino acid amides as new substrates for α-amino--caprolactam racemase from Achromobacter obae |
journal |
Journal of Molecular Catalysis B: Enzymatic |
Activity |
5.1.1.15 |
Family |
5.1.1.15 |
sel |
selected |
ui |
jghbhilfj |
year |
(2005) |
volume |
36 |
number |
1 |
pages |
22-29 |
| |
abstract |
Amino acid amide racemizing activity was discovered in -amino--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. |
last changed |
2007/12/20 18:21 |
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