Consider the following questions about glutamate dehydrogenase.(a) The reaction has NH3 as a reactant, instead of NH4+, which is far more abundant at physiological pH. Why is NH3 preferred?(b) Glutamate dehydrogenase has a KM for ammonia (NH3) of ~1 mM.However, at physiological pH, the dominant ionic species is ammoniumion, NH4+ (pKa = 9.2). Calculate the velocity (as a fraction of Vmax) that would be achieved by glutamate dehydrogenase if the total intracellularammonia concentration (NH3 + NH4+) is 100 mM (approximatephysiological concentration). Assume a mitochondrial matrix pH of 8.0.(c) The thermodynamic equilibrium for the reaction greatly favors aketoglutarate reduction; yet in mitochondria the enzyme acts primarily to oxidize glutamate to a-ketoglutarate. Explain.(d) Propose a reasonable mechanism for this reaction.

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Chapter1: Biochemistry: An Evolving Science
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Consider the following questions about glutamate dehydrogenase.
(a) The reaction has NH3 as a reactant, instead of NH4+, which is far more abundant at physiological pH. Why is NH3 preferred?
(b) Glutamate dehydrogenase has a KM for ammonia (NH3) of ~1 mM.
However, at physiological pH, the dominant ionic species is ammonium
ion, NH4+ (pKa = 9.2). Calculate the velocity (as a fraction of Vmax) that would be achieved by glutamate dehydrogenase if the total intracellular
ammonia concentration (NH3 + NH4+) is 100 mM (approximate
physiological concentration). Assume a mitochondrial matrix pH of 8.0.
(c) The thermodynamic equilibrium for the reaction greatly favors aketoglutarate reduction; yet in mitochondria the enzyme acts primarily to oxidize glutamate to a-ketoglutarate. Explain.
(d) Propose a reasonable mechanism for this reaction.

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