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The fission yeast Pvg1p has galactose‐specific pyruvyltransferase activity
Author(s) -
Yoritsune Ken-ichi,
Matsuzawa Tomohiko,
Ohashi Takao,
Takegawa Kaoru
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.02.016
Subject(s) - schizosaccharomyces pombe , yeast , galactose , recombinant dna , glycan , biochemistry , chemistry , substrate (aquarium) , schizosaccharomyces , stereochemistry , nuclear magnetic resonance spectroscopy , phosphoenolpyruvate carboxykinase , saccharomyces cerevisiae , biology , enzyme , gene , glycoprotein , ecology
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 ( p NP‐β‐Gal) was used as a substrate, the structure of the recombinant Pvg1p product was determined to be p NP‐PvGal by one‐ and two‐dimensional NMR spectroscopy. The recombinant Pvg1p transferred pyruvyl residues from phosphoenolpyruvate specifically to β‐linked galactose.