D-Aminoacylase from Alcaligenes faecalis possesses novel activities on D-methionine

  • Bioorg Med Chem. 1994 Jan;2(1):1-5. doi: 10.1016/s0968-0896(00)82195-1.
H P Chen  1 ,  S H Wu ,  K T Wang
Affiliations
  • 1. Department of Biochemistry, China Medical College, Taichung, Taiwan.
PMID: 7922115 DOI: 10.1016/s0968-0896(00)82195-1
Abstract

D-Aminoacylase isolated from Alcaligenes faecalis DA1 has a great potential for future application in D-amino acids production. This paper reports for the first time that D-aminoacylase can reverse the catalysis direction on D-Met and deacylate N-Ac-D-Met-OMe and N-Ac-D-Met-Gly. The results provide important insights regarding the binding and affinity of substrates to the active site of this enzyme. Based on a systematic study of kinetic properties and relative reactivities for a broad range of substrates, a model to elucidate the reaction mechanism is proposed.

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