Dynamic kinetic resolution of amino acid amide catalyzed by D-aminopeptidase and alpha-amino-epsilon-caprolactam racemase.
Amino acid amide racemizing activity was discovered in alpha-amino-epsilon-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 degrees 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.
Asano
Yasuhisa
Y
Biotechnology Research Center, Toyama Prefectural University, 5180 Kurokawa, Kosugi, Toyama 939-0398, Japan. asano@pu-toyama.ac.jp
Yamaguchi
Shigenori
S
D042402:Achromobacter / Q000201:enzymology; D000577:Amides / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D000591:Amino Acid Isomerases / Q000737:chemistry* / Q000378:metabolism; D000596:Amino Acids / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D000626:Aminopeptidases / Q000737:chemistry* / Q000378:metabolism; D001409:Bacillus cereus / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D007700:Kinetics; D020621:Ochrobactrum anthropi / Q000201:enzymology; D013237:Stereoisomerism; D013379:Substrate Specificity
D000577:Amides; D000596:Amino Acids; D001426:Bacterial Proteins; D000626:Aminopeptidases; D000591:Amino Acid Isomerases; C036861:aminocaprolactam racemase