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Article

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

Chemical communications (Cambridge, England) - 21 Nov 2010

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

Abstract excerpt

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...

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Source

Identifiers

PMID: 20924508
DOI: 10.1039/c0cc02768e

Genes

PAM

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20924508-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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