Enolase catalyzed beta,gamma-alpha,beta isomerization of 2-phospho-3-butenoic acid to (Z)-phosphoenol-alpha-ketobutyrate.
2-Phospho-3-butenoic acid was synthesized and found to be a substrate for both yeast and rabbit muscle enolase (EC 4.2.1.11). Enolase catalyzes the isomerization of 2-phospho-3-butenoic acid to (Z)-phosphoenol-alpha-ketobutyrate, a beta,gamma-alpha,beta isomerization. Nuclear magnetic resonance studies on the product indicate only one isomer is formed. This reaction provides indirect evidence in further support of a carbanion intermediate for the enolase reaction. 2-Phospho-3-butenoic acid is also a good competitive inhibitor of both yeast and rabbit muscle pyruvate kinase (EC 2.7.1.40).
D000818:Animals; D002087:Butyrates / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D009132:Muscles / Q000201:enzymology; D009943:Organophosphorus Compounds / Q000494:pharmacology*; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000037:antagonists & inhibitors; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D002087:Butyrates; D009943:Organophosphorus Compounds; D011770:Pyruvate Kinase; D010751:Phosphopyruvate Hydratase