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Article

Directed evolution of N-acetylneuraminic acid aldolase to catalyze enantiomeric aldol reactions.

Bioorganic & medicinal chemistry - 1 May 2003

Wada Masaru, Hsu Che-Chang, Franke Dirk, Mitchell Michael, Heine Andreas, Wilson Ian, Wong Chi-Huey

Abstract excerpt

Expanding the scope of substrate specificity and stereoselectivity is of current interest in enzyme catalysis. Using error-prone PCR for in vitro directed evolution, the Neu5Ac aldolase from Escherichia coli has been altered to improve its catalytic activity toward enantiomeric substrates including N-acetyl-L-mannosamine and L-arabinose to produce L-sialic acid and L-KDO, the mirror-image sugars of the...

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PMID: 12670660
DOI: 10.1016/s0968-0896(03)00052-x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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