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A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: Structure of the yeast enzyme complexee with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.BA resolution
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Mechanism of enolase: The crystal structure of enolase-Mg2+-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2A resolution
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0029153382
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Preparation by site-directed mutagenesis and characterization of the E211Q mutant of yeast enolase 1
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Sangadala VS, Glover GVC, Robson RL, Holland MJ, Lebioda L, Brewer JM: Preparation by site-directed mutagenesis and characterization of the E211Q mutant of yeast enolase 1. Biochem Biaphys Ada 1995, 1251:23-31. The is the first report on the properties at Glu21lGln enolase. The mutant enzyme was purified Irom a yeast expression system. The data show a strong UV difference spectrum characteristic of the ionized form of TSF. A smaller change in the UV spectrum which developed after a significant time delay was interpreted as the ionization step- Experimental results in the TSP assay ara in agreement with those reported for Glu211 Gin enolase purified from the E. coli expression system [20"].
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Toward identification of acid/base catalysts in the active site of enolase: Comparison of the properties of K345A, E168Q, and E211Q variants
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Analogs of phosphoenolpyruvate. Substrate specificities of enolase and pyruvate kinase from rabbit muscle
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A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids
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