FEBS Letters 2013-04-02

The fission yeast Pvg1p has galactose-specific pyruvyltransferase activity.

Ken-ichi Yoritsune, Tomohiko Matsuzawa, Takao Ohashi, Kaoru Takegawa

Index: FEBS Lett. 587(7) , 917-21, (2013)

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Abstract

N-Glycan from the fission yeast Schizosaccharomyces pombe contains outer-chain pyruvic acid 4,6-ketal-linked galactose (PvGal). Here, we characterized a putative S. pombe pyruvyltransferase, Pvg1p, reported to be essential for biosynthesis of PvGal. When p-nitrophenyl-β-Gal (pNP-β-Gal) was used as a substrate, the structure of the recombinant Pvg1p product was determined to be pNP-PvGal by one- and two-dimensional NMR spectroscopy. The recombinant Pvg1p transferred pyruvyl residues from phosphoenolpyruvate specifically to β-linked galactose.Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.