title: Priming ammonia lyases and aminomutases for industrial and therapeutic applications.
abstract: 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.
authors.affiliation: Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
authors.forename: Matthew M
authors.initials: MM
authors.lastname: Heberling
authors.forename: Bian
authors.initials: B
authors.lastname: Wu
authors.forename: Sebastian
authors.initials: S
authors.lastname: Bartsch
authors.forename: Dick B
authors.initials: DB
authors.lastname: Janssen
mesh_terms: D000642:Ammonia-Lyases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D004345:Drug Industry / Q000379:methods*; D005656:Fungal Proteins / Q000737:chemistry; D007218:Industrial Microbiology / Q000379:methods*; D019751:Intramolecular Transferases / Q000737:chemistry*; D053858:Metabolic Networks and Pathways; D015202:Protein Engineering / Q000379:methods*
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; D000642:Ammonia-Lyases; D019751:Intramolecular Transferases