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A protonated histidine residue in the active site of aspartate transcarbamoylase, ATCase, is thought to be...

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Chemistry

A protonated histidine residue in the active site of aspartatetranscarbamoylase, ATCase, is thought to be important instabilizing the transition state of the bound substrate.

A) Sketch a graph showing the pH dependence of the catalyticrate, assuming that this interaction is essential and dominates thepH-activity profile of the enzyme. Provide the biochemical basisfor your graph.

B) The ATCase mechanism is known to proceed via an orderedmechanism. Draw a Cleland notation diagram showing how thisreaction proceeds. Abbreviate the second substrate as CP. Twoproducts are formed.  

Thank you!

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