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E. coli pyruvate dehydrogenase binding constant and maximum velocity values have been reported as Km = 0.3 mM and Vmax = 5,500 kat/mol (37 degrees C, pH = 7.6, 5 microM pyruvate, and 3 mg/L protein). The multienzyme complex exhibits postive cooperative binding (Hill constant = 1.9)<ref>Bisswanger, H. Substrate specificity of the pyruvate dehydrogenase complex from escherichia coli. J Biol Chem. 1981. Jan 25;256(2):815-822.</ref>. | E. coli pyruvate dehydrogenase binding constant and maximum velocity values have been reported as Km = 0.3 mM and Vmax = 5,500 kat/mol (37 degrees C, pH = 7.6, 5 microM pyruvate, and 3 mg/L protein). The multienzyme complex exhibits postive cooperative binding (Hill constant = 1.9)<ref>Bisswanger, H. Substrate specificity of the pyruvate dehydrogenase complex from escherichia coli. J Biol Chem. 1981. Jan 25;256(2):815-822.</ref>. | ||
==References== | |||
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