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TitleEngineered Phenylalanine Ammonia-Lyases for the Enantioselective Synthesis of Aspartic Acid Derivatives.
Journal, issue, pagesAngew Chem Int Ed Engl, Vol. 63, Issue 31, Page e202406008, Year 2024
Publish dateJul 29, 2024
AuthorsIvan Buslov / Sarah Desmons / Yoan Duhoo / Xile Hu /
PubMed AbstractBiocatalytic hydroamination of alkenes is an efficient and selective method to synthesize natural and unnatural amino acids. Phenylalanine ammonia-lyases (PALs) have been previously engineered to ...Biocatalytic hydroamination of alkenes is an efficient and selective method to synthesize natural and unnatural amino acids. Phenylalanine ammonia-lyases (PALs) have been previously engineered to access a range of substituted phenylalanines and heteroarylalanines, but their substrate scope remains limited, typically including only arylacrylic acids. Moreover, the enantioselectivity in the hydroamination of electron-deficient substrates is often poor. Here, we report the structure-based engineering of PAL from Planctomyces brasiliensis (PbPAL), enabling preparative-scale enantioselective hydroaminations of previously inaccessible yet synthetically useful substrates, such as amide- and ester-containing fumaric acid derivatives. Through the elucidation of cryo-electron microscopy (cryo-EM) PbPAL structure and screening of the structure-based mutagenesis library, we identified the key active site residue L205 as pivotal for dramatically enhancing the enantioselectivity of hydroamination reactions involving electron-deficient substrates. Our engineered PALs demonstrated exclusive α-regioselectivity, high enantioselectivity, and broad substrate scope. The potential utility of the developed biocatalysts was further demonstrated by a preparative-scale hydroamination yielding tert-butyl protected l-aspartic acid, widely used as intermediate in peptide solid-phase synthesis.
External linksAngew Chem Int Ed Engl / PubMed:38713131
MethodsEM (single particle)
Resolution2.17 Å
Structure data

19897

9eq5

EMDB-19897, PDB-9eq5:
CryoEM Structure of Phenylalanine Ammonia Lyase from Planctomyces brasiliencis
Method: EM (single particle) / Resolution: 2.17 Å

Chemicals

ChemComp-PPH:
[(1R)-1-amino-2-phenylethyl]phosphonic acid

Source
  • Rubinisphaera brasiliensis DSM 5305 (bacteria)
  • rubinisphaera brasiliensis (bacteria)
KeywordsLYASE / Phenylalanine catabolism Lyase

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