The fission yeast Pvg1p has galactose-specific pyruvyltransferase activity

Autor:	Takao Ohashi, Kaoru Takegawa, Tomohiko Matsuzawa, Ken Ichi Yoritsune
Rok vydání:	2012
Předmět:	Pyruvyltransferase Magnetic Resonance Spectroscopy Biophysics Biology Biochemistry law.invention Substrate Specificity Fungal Proteins Phosphoenolpyruvate chemistry.chemical_compound Biosynthesis Aldehyde-Ketone Transferases Structural Biology law Cell Wall Transferases Pyruvic Acid Schizosaccharomyces Genetics Molecular Biology Pyruvylated galactose Chromatography High Pressure Liquid Pyruvyltransferase activity Galactose Biological Transport Cell Biology biology.organism_classification Galactosyltransferases Yeast Recombinant Proteins Kinetics N-Glycan chemistry Schizosaccharomyces pombe Mutation Recombinant DNA Pyruvic acid Schizosaccharomyces pombe Proteins Phosphoenolpyruvate carboxykinase
Zdroj:	FEBS letters. 587(7)
ISSN:	1873-3468
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e7c8c2be0bbba05a382c17c9c41e262 https://pubmed.ncbi.nlm.nih.gov/23422075 Zobrazit plný text záznamu Plný text