Aspartate Transcarbamoylase (ATCase): Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Revision as of 02:48, 23 April 2014 view source Andre Agassi (talk \| contribs) 30 edits No edit summary ← Older edit		Revision as of 02:52, 23 April 2014 view source Andre Agassi (talk \| contribs) 30 edits No edit summary Newer edit →
Line 9:		Line 9:

	== Mechanism ==		== Mechanism ==
	ATCase displays features of a concerted mechanism due to the fact that changes in the enzyme are "all or none". In Michaelis-Menten kinetics, ATCase's curve is sigmoidal exemplifying a union of the R (active) and T (tense) states. High concentrations of CTP shift the curve right towards the T state, whereas high concentrations of ATP shift the curve left towards the R state.		ATCase displays features of a concerted mechanism due to the fact that changes in the enzyme are "all or none". In [http://en.wikipedia.org/wiki/Michaelis–Menten_kinetics Michaelis-Menten kinetics], ATCase's curve is sigmoidal exemplifying a union of the R (active) and T (tense) states. High concentrations of CTP shift the curve right towards the T state, whereas high concentrations of ATP shift the curve left towards the R state.