L-carnitine via enzyme-catalyzed oxidative kinetic resolution

• Published in: Bioorganic & medicinal chemistry Vol. 2; no. 6; pp. 415 - 420
• Main Authors: Ditullio, Dennis, Anderson, David, Chen, Ching-Shih, Sih, Charles J.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.06.1994
• Subjects: Acinetobacter calcoaceticus - genetics; Acinetobacter calcoaceticus - growth & development; Acinetobacter calcoaceticus - metabolism; Carbon Radioisotopes; Carnitine - chemistry; Carnitine - isolation & purification; Carnitine - metabolism; Kinetics; Oxidation-Reduction; Radioisotope Dilution Technique; Stereoisomerism; Time Factors
• ISSN: 0968-0896; 1464-3391
• DOI: 10.1016/0968-0896(94)80009-X

l-Carnitine of high optical purity was prepared via kinetic resolution using a mutant strain of Acinetobacter calcoaceticus ATCC 39647, This organism preferentially metabolized the d-enantiomer of the racemate to furnish l-carnitine. Recovery of l-carnitine was 93 %, providing a total weight yield of 46.5 % in 92% enantiomeric excess. The mode of degradation of carnitine was shown to proceed via a monooxygenase-catalyzed oxidative cleavage resulting in the formation of trimethylamine and malic acid. The data suggest that the stereoselective metabolism of dl-carnitine is probably the result of differential permeability of the cell membrane towards the optical antipodes. L-Carnitine of high optical purity was prepared via kinetic resolution using a mutant strain of Acinetobacter calcoaceticus ATCC 39647. This organism preferentially metabolized the D-enantiomer of the racemate to furnish L-carnitine. Recovery of L-carnitine was 93%, providing a total weight yield of 46.5% in 92% enantiomeric excess. The mode of degradation of carnitine was shown to proceed via a monooxygenase-catalyzed oxidative cleavage resulting in the formation of trimethylamine and malic acid.