Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase

Bian Wu; Wiktor Szymański; Hein J Wijma; Ciprian G Crismaru; Stefaan de Wildeman; Gerrit J Poelarends; Ben L Feringa; Dick B Janssen

doi:10.1039/c0cc02768e

Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase

Chem Commun (Camb). 2010 Nov 21;46(43):8157-9. doi: 10.1039/c0cc02768e. Epub 2010 Oct 5.

Authors

Bian Wu¹, Wiktor Szymański, Hein J Wijma, Ciprian G Crismaru, Stefaan de Wildeman, Gerrit J Poelarends, Ben L Feringa, Dick B Janssen

Affiliation

¹ Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.

PMID: 20924508
DOI: 10.1039/c0cc02768e

Abstract

By replacing a single active-site residue Cys107 with Ser in phenylalanine aminomutase (PAM), the enzyme gained tyrosine aminomutase (TAM) activity while retaining PAM activity and high enantioselectivity. This engineered enantioselective TAM also catalyzed formation of β-tyrosine from p-coumaric acid and may prove to be useful for the synthesis of enantiopure β-tyrosine and its derivatives.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amino Acid Substitution
Ammonia-Lyases / chemistry
Ammonia-Lyases / metabolism
Catalytic Domain
Intramolecular Transferases / chemistry*
Intramolecular Transferases / genetics
Intramolecular Transferases / metabolism
Kinetics
Molecular Sequence Data
Mutation
Protein Engineering*
Protein Structure, Tertiary
Sequence Alignment
Stereoisomerism
Tyrosine / biosynthesis*
Tyrosine / chemistry

Substances

Tyrosine
Ammonia-Lyases
Intramolecular Transferases