Enzymatic preparation of optically active silicon-containing amino acids and their application

  • Takuo Kawamoto
  • Hayato Yamanaka
  • Atsuo Tanaka


Optically active 3-trimethyl silylalanine (TMS-Ala) was prepared by hydrolysis of N-acetyl-dl-TMS-Ala catalyzed by acylase I (aminoacylase; N-acylamino-acid amidohydrolase, EC3.5.1.14). Acylase I from porcine kidney (PKA) was found to be more effective than that from Aspergillus melleus in the preparation of l-TMS-Ala. Under the optimized conditions, optically pure l-TMS-Ala (>99% enantiomeric excess, ee) was obtained with a 72% yield. Furthermore, a highly optically pure d-TMS-Ala (96% ee) could also be obtained with a 76% yield by chemical hydrolysis of the residual substrate. Enzymatic synthesis of peptides containing TMS-Ala was also attempted in ethyl acetate. Benzyloxycarbonyl (Z)-l-TMS-Ala served as the substrate for thermolysin, whereas l-TMS-Ala-OMe was inactive as the amino component. In the case of inhibitory activity of dipeptides toward thermolysin, l-Leu-(l-TMS-Ala) was found to be a more potent inhibitor than l-Leu-l-Leu, which is known to be one of the most effective inhibitors of thermolysin among the dipeptides consisting of natural aminoacids.

Index Entries

Enzymatic preparation silicon-containing amino acid trimethylsilylalanine acylase I dipeptide thermolysin inhibitor 


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Copyright information

© Humana Press Inc. 2000

Authors and Affiliations

  1. 1.Department of Synthetic Chemistry and Biological Chemistry, Graduate School of EngineeringKyoto UniversityKyotoJapan

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