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Article

A rationally engineered yeast pyruvyltransferase Pvg1p introduces sialylation-like properties in neo-human-type complex oligosaccharide.

Scientific reports - 19 May 2016

Higuchi Yujiro, Yoshinaga Sho, Yoritsune Ken-Ichi, Tateno Hiroaki, Hirabayashi Jun, Nakakita Shin-Ichi, Kanekiyo Miho, Kakuta Yoshimitsu, Takegawa Kaoru

Abstract excerpt

Pyruvylation onto the terminus of oligosaccharide, widely seen from prokaryote to eukaryote, confers negative charges on the cell surface and seems to be functionally similar to sialylation, which is found at the end of human-type complex oligosaccharide. However, detailed molecular mechanisms underlying pyruvylation have not been clarified well. Here, we first determined the crystal structure of fission yeast...

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Identifiers

PMID: 27194449
DOI: 10.1038/srep26349
PMCID: PMC4872226

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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