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Enzymatic synthesis of l -6-hydroxynorleucine

Authors :
Clyde G. McNamee
Bang-Chi Chen
Ronald L. Hanson
Gus A. Kodersha
Amit Banerjee
Mark D. Schwinden
Ramesh N. Patel
David R. Kronenthal
David B. Brzozowski
Bharat P. Patel
Laszlo J. Szarka
Source :
Bioorganic & Medicinal Chemistry. 7:2247-2252
Publication Year :
1999
Publisher :
Elsevier BV, 1999.

Abstract

L-6-Hydroxynorleucine, a key chiral intermediate used for synthesis of a vasopeptidase inhibitor, was prepared in 89% yield and > 99% optical purity by reductive amination of 2-keto-6-hydroxyhexanoic acid using glutamate dehydrogenase from beef liver. In an alternate process, racemic 6-hydroxynorleucine produced by hydrolysis of 5-(4-hydroxybutyl)hydantoin was treated with D-amino acid oxidase to prepare a mixture containing 2-keto-6-hydroxyhexanoic acid and L-6-hydroxynorleucine followed by the reductive amination procedure to convert the mixture entirely to L-6-hydroxynorleucine, with yields of 91 to 97% and optical purities of > 99%.

Details

ISSN :
09680896
Volume :
7
Database :
OpenAIRE
Journal :
Bioorganic & Medicinal Chemistry
Accession number :
edsair.doi.dedup.....aa36745b91b228a999b9a2d435e462b8