Open AccessFrom Enzymes to “Designer Bugs” in Reductive Amination: A New Process for the Synthesis of L‐ tert ‐Leucine Using a Whole Cell‐Catalyst
Author(s) -
Menzel A.,
Werner H.,
Altenbuchner J.,
Gröger H.
Publication year - 2004
Publication title -
engineering in life sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.547
H-Index - 57
eISSN - 1618-2863
pISSN - 1618-0240
DOI - 10.1002/elsc.200402162
Subject(s) - formate dehydrogenase , reductive amination , formate , amination , catalysis , leucine , chemistry , cofactor , combinatorial chemistry , enantiomeric excess , amino acid , organic chemistry , enzyme , enantioselective synthesis , biochemistry
A whole‐cell‐catalyst for the asymmetric reductive amination of α‐keto acids has been developed and applied for the synthesis of the non‐proteinogenic α‐amino acid L‐ tert ‐leucine. Besides the economical whole‐cell catalyst, bearing a leucine dehydrogenase from Bacillus cereus and a formate dehydrogenase from Candida boidinii , it is further advantageous that there is no need for the addition of external cofactor. The desired product is formed with high conversion and an enantiomeric purity of > 99 % ee.