LEcta GmbH

Leipzig, Germany

LEcta GmbH

Leipzig, Germany
SEARCH FILTERS
Time filter
Source Type

Heberling M.M.,University of Groningen | Wu B.,University of Groningen | Bartsch S.,LEcta GmbH | Janssen D.B.,University of Groningen
Current Opinion in Chemical Biology | Year: 2013

Ammonia lyases (AL) and aminomutases (AM) are emerging in green synthetic routes to chiral amines and an AL is being explored as an enzyme therapeutic for treating phenylketonuria and cancer. Although the restricted substrate range of the wild-type enzymes limits their widespread application, the non-reliance on external cofactors and direct functionalization of an olefinic bond make ammonia lyases attractive biocatalysts for use in the synthesis of natural and non-natural amino acids, including β-amino acids. The approach of combining structure-guided enzyme engineering with efficient mutant library screening has extended the synthetic scope of these enzymes in recent years and has resolved important mechanistic issues for AMs and ALs, including those containing the MIO (4-methylideneimidazole-5-one) internal cofactor. © 2013.

Loading LEcta GmbH collaborators
Loading LEcta GmbH collaborators