Dynamic kinetic resolution of amino acid amide catalyzed by D-aminopeptidase and alpha-amino-epsilon-caprolactam racemase

J Am Chem Soc. 2005 Jun 1;127(21):7696-7. doi: 10.1021/ja050300m.

Abstract

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.

MeSH terms

  • Achromobacter / enzymology
  • Amides / chemistry*
  • Amides / isolation & purification
  • Amides / metabolism
  • Amino Acid Isomerases / chemistry*
  • Amino Acid Isomerases / metabolism
  • Amino Acids / chemistry*
  • Amino Acids / isolation & purification
  • Amino Acids / metabolism
  • Aminopeptidases / chemistry*
  • Aminopeptidases / metabolism
  • Bacillus cereus / enzymology
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Catalysis
  • Kinetics
  • Ochrobactrum anthropi / enzymology
  • Stereoisomerism
  • Substrate Specificity

Substances

  • Amides
  • Amino Acids
  • Bacterial Proteins
  • Aminopeptidases
  • Amino Acid Isomerases
  • aminocaprolactam racemase