Talk:Glutamate dehydrogenase

Merger proposal

 * Oppose – if glutamate dehydrogenase 1 were merged into this article, then glutamate dehydrogenase 2 would also need to be merged.  Including two large GNF Protein box templates in the same article that already includes three enzyme templates would overwhelm the text.  Boghog (talk) 14:03, 11 October 2011 (UTC)

Missing sources/possibly incorrect info
I'm currently studying a course on the subject and it seems that the claim that the reverse reaction that binds ammonium to alfaketoglutarate doesn't happen in mammals is false, as it is the only way for cells to lower levels of free ammonium ions? There's also no source given for this claim and many online sources indeed state this reaction as primary regulator of excess nitrogen.

Notice : the opposite expression prefered
you have presented the ability of "Glutamate dehydrogenase" to catalyze the reverse direction in a little bit confusing way: as if you was showing mammals to have "exceptional" inability of a reverse catalysis, whereas I would prefer if you present the ability of lower organisms (prokaryotes and some plants) to catalyze "two directions" as something exceptional ...

in other words: it is more readily accepted that the enzyme catalyze only forward reaction.and having some species catalyzing two opposite reactions by the same enzyme is the weird thing. — Preceding unsigned comment added by Yasir muhammed ali (talk • contribs) 11:47, 8 April 2016 (UTC)

the irreversibility of glutamate DH in vertebrates:
It seems this apply only to the isoenzyme concerned with urea cycle, not the iso enzyme of the nervous system (GLUD2) Which is concerned with recycling of glutamate neurotransmitter, and is reversible in action. — Preceding unsigned comment added by Yasir muhammed ali (talk • contribs) 18:45, 10 April 2016 (UTC)

Not exactly on the same topic, but about reversibility: the intro paragraph implies that the enzyme kinetics (michaelis constant) is why this reaction does not go in reverse. This is not how equilibrium works. Kinetics doesn't determine direction of reaction, but rather the speed at which it goes. Only thermodynamic considerations determine the direction of the reaction. The energy of binding to enzyme (Km) does not matter because in both the initial and final states the enzyme is not bound or modified (definition of a catalyst). Hess' law tells us that we only consider initial and final states to figure the thermodynamics of the reaction. Wikipedia should probably not be saying things that go against physical laws. — Preceding unsigned comment added by Tooochinoise (talk • contribs) 18:48, 18 May 2018 (UTC)