Yeast enolase carboxyl modification using Woodward's reagent K.
Yeast enolase is inactivated by Woodward's reagent K. Substantial protection is afforded by binding of 1 mol of "conformational" metal ion/subunit. Inactivation is correlated with modification of 13 carboxyl groups/subunit in the absence of conformational metal ion and 17 in its presence. Ten tryptic peptides labeled by Woodward's reagent K can be isolated, mostly from the C-terminal half of the protein. The changes in reactivity of these peptides produced by conformational metal ion suggest direct coordination to Glu-181 together with a contraction of the protein.
D000596:Amino Acids / Q000032:analysis; D007555:Isoxazoles / Q000494:pharmacology*; D007700:Kinetics; D010080:Oxazoles / Q000494:pharmacology*; D010446:Peptide Fragments / Q000032:analysis; D010751:Phosphopyruvate Hydratase / Q000037:antagonists & inhibitors*; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000596:Amino Acids; D007555:Isoxazoles; D010080:Oxazoles; D010446:Peptide Fragments; C009686:N-ethyl-5-phenylisoxazolium-3'-sulfonate; D010751:Phosphopyruvate Hydratase