BioChem - DOS

Reductive amination by recombinant Escherichia coli: Whole cell biotransformation of 2-keto-3-methylvalerate to L-isoleucine

Journal of biotechnology

Lorenz, E.; Klatte, S.; Wendisch, V.F.

A whole cell biotransformation system for reductive amination has been studied in recombinant Escherichia coli cells. Reductive amination of 2-keto-3-methylvalerate to l-isoleucine by a two-enzyme-cascade was achieved by overproduction of endogenous l-alanine dependent transaminase AvtA and heterologous l-alanine dehydrogenase from Bacillus subtilis in recombinant E. coli. Up to 100mM l-isoleucine were produced from 100mM 2-keto-3-methylvalerate and 100mM ammonium sulfate. Regeneration of NADH as cofactor in the whole cell system was driven by glucose catabolism. The effects of defined gene deletions in the central carbon metabolism on biotransformation were tested. Strains lacking the NuoG subunit of NADH:ubiquinone oxidoreductase (complex I) or aceA encoding the glyoxylate cycle enzyme isocitrate lyase exhibited increased biotransformation rates.

2013

Elsevier Science Publishers

0168-1656

1873-4863

168

3

pp.289-294

10.1016/j.jbiotec.2013.06.014

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART67395003

Whole cell biotransformation; Reductive amination; 2-keto-3-methylvalerate; Transaminase; l-Alanine dehydrogenase