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From the same journal

An Improved Racemase/Acylase Biotransformation for the Preparation of Enantiomerically Pure Amino Acids

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Published copy (DOI)

Author(s)

  • S. Baxter
  • D.J. Campopiano
  • S. Royer
  • G. Grogan
  • K.E. Holt-Tiffin
  • I.N. Taylor
  • F. Brown
  • I.G. Fotheringham

Department/unit(s)

Publication details

JournalJournal of the American Chemical Society
DatePublished - 28 Nov 2012
Issue number47
Volume134
Number of pages4
Pages (from-to)19310-19313
Original languageEnglish

Abstract

Using directed evolution, a variant N-acetyl amino acid racemase (NAAAR G291D/F323Y) has been developed with up to 6-fold higher activity than the wild-type on a range of N-acetylated amino acids. The variant has been coupled with an enantiospecific acylase to give a preparative scale dynamic kinetic resolution which allows 98% conversion of N-acetyl-dl-allylglycine into d-allylglycine in 18 h at high substrate concentrations (50 g L). This is the first example of NAAAR operating under conditions which would allow it to be successfully used on an industrial scale for the production of enantiomerically pure α-amino acids. X-ray crystal analysis of the improved NAAAR variant allowed a comparison with the wild-type enzyme. We postulate that a network of novel interactions that result from the introduction of the two side chains is the source of improved catalytic performance. © 2012 American Chemical Society.

    Research areas

  • GENE, RACEMIZATION, ESCHERICHIA-COLI, DYNAMIC KINETIC RESOLUTION, ENZYME, AMYCOLATOPSIS SP TS-1-60, ASYMMETRIC-SYNTHESIS, ENOLASE SUPERFAMILY, O-SUCCINYLBENZOATE SYNTHASE, EVOLUTION

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