The fission yeast Pvg1p has galactose-specific pyruvyltransferase activity.
FEBS Lett.2013 Apr 2;587(7):917-21. Epub 2013 Feb 16
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摘要
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.
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基因功能
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原始数据
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文献解读
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