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Article

Probing the roles of conserved residues in uridyltransferase domain of Escherichia coli K12 GlmU by site-directed mutagenesis.

Carbohydrate research - 2 Sept 2015

Wang Shuaishuai, Fu Xuan, Liu Yunpeng, Liu Xian-wei, Wang Lin, Fang Junqiang, Wang Peng George

Abstract excerpt

N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme that catalyzes both acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthesis pathway. Our previous study demonstrated that the uridyltransferase domain of GlmU (tGlmU) exhibited a flexible substrate specificity, which could be further applied in unnatural sugar nucleotides preparation. However, the...

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Identifiers

PMID: 26101844
DOI: 10.1016/j.carres.2015.05.007

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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