Priming ammonia lyases and aminomutases for industrial and therapeutic applications

Matthew M. Heberling, Bian Wu, Sebastian Bartsch, Dick B. Janssen*

*Bijbehorende auteur voor dit werk

Onderzoeksoutput: Review articlepeer review

74 Citaten (Scopus)
159 Downloads (Pure)


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 beta-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.

Originele taal-2English
Pagina's (van-tot)250-260
Aantal pagina's11
TijdschriftCurrent Opinion in Chemical Biology
Nummer van het tijdschrift2
StatusPublished - apr.-2013

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