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Article

Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val-251.

The Journal of biological chemistry - 22 Apr 2011

Chou Chien-Yu, Ko Tzu-Ping, Wu Kuan-Jung, Huang Kai-Fa, Lin Chun-Hung, Wong Chi-Huey, Wang Andrew H-J

Abstract excerpt

In a recent directed-evolution study, Escherichia coli D-sialic acid aldolase was converted by introducing eight point mutations into a new enzyme with relaxed specificity, denoted RS-aldolase (also known formerly as L-3-deoxy-manno-2-octulosonic acid (L-KDO) aldolase), which showed a preferred s...

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Identifiers

PMID: 21270125
DOI: 10.1074/jbc.M110.179465
PMCID: PMC3077606

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-21270125-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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