title: [Identification of an essential glutamate residue in the 3-phosphoglycerate kinase of yeast].
abstract: The incorporation of nitrotyrosine into 3-phosphoglycerate kinase activated by carbodiimide results in the chemical modification of a single essential residue. After total proteolytic digestion, isolation of the dipeptide gamma Glu-NO2 Tyr by immuno-affinity chromatography indicates the implication of a glutamyl residue. It is interesting to point out the applicability of the method described for the purification of peptides containing carboxyl residues.
mesh_terms: D001665:Binding Sites; D002234:Carbodiimides / Q000494:pharmacology; D055598:Chemical Phenomena; D002621:Chemistry; D004357:Drug Synergism; D005971:Glutamates / Q000302:isolation & purification; D010735:Phosphoglycerate Kinase / Q000032:analysis* / Q000037:antagonists & inhibitors; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D014443:Tyrosine / Q000031:analogs & derivatives / Q000494:pharmacology
chemical_list: D002234:Carbodiimides; D005971:Glutamates; D014443:Tyrosine; D010735:Phosphoglycerate Kinase
vernacular_title: Identification du groupement glutamique essentiel de la 3-phosphoglycérate kinase de levure.