Alanine aminotransferase catalyzes the transamination of alanine and $\alpha$-ketoglutarate to pyruvate and glutamate, while aspartate transaminase converts aspartate and $\alpha$-ketoglutarate to oxaloacetate and glutamate. If you have a 50.0-mL reaction volume containing 0.100 M alanine, $\alpha$-ketoglutarate, glutamate, and oxaloacetate, what will the equilibrium concentration of aspartate be? Assume an equilibrium constant of 1.0 for both enzyme-catalyzed reactions.

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The Answer of Alanine aminotransferase catalyzes the transamination of alanine and $\alpha$-ketoglutarate to pyruvate and glutamate, while aspartate transaminase converts aspartate and $\alpha$-ketoglutarate to oxaloacetate and glutamate. If you have a 50.0-mL reaction volume containing 0.100 M alanine, $\alpha$-ketoglutarate, glutamate, and oxaloacetate, what will the equilibrium concentration of aspartate be? Assume an equilibrium constant of 1.0 for both enzyme-catalyzed reactions.

Alanine Aminotransferase Catalyzes the Transamination of Alanine And α\alphaα -Ketoglutarate to Pyruvate and Glutamate, While Aspartate Transaminase Converts Aspartate

Alanine Aminotransferase Catalyzes the Transamination of Alanine And $\alpha$ -Ketoglutarate to Pyruvate and Glutamate, While Aspartate Transaminase Converts Aspartate