ATCase activity is controlled by affecting the equilibrium between the T and R s

Question

ATCase activity is controlled by affecting the equilibrium between the T and R states. Substrate binding favors the R state, whereas binding of CTP — the feedback inhibitor of ATCase — favors the T state.

a) Suppose that the interfaces of the catalytic subunits of ATCase contain juxtaposed tyrosine residues within the consensus sequence of a cellular tyrosine kinase. How would activation of this kinase affect ATCase activity?

b) Now suppose that one of each pair of tyrosine is replace by a lysine residue, resulting in interfaces between the catalytic subunits containing juxtaposed tyrosine and lysine residues. How would activation of the kinase affect ATCase activity?

Explanation / Answer

ANS.A tyrosine kinase is an enzyme that can transfer a phosphate group a ATP to protein in a cell. and it regulate the axon path finding and development of cardiovascular system as well as the migration of the neuron cells.

ANS.ATcase was reacted with nitromethane to form a colored nitrotyrosine group ineach of its catalytic chains.the absorption by this reporter group is depends on its immediate environment.an essenstial lysine residue at each catalytic site also was modified enzyme were then combined with native trimmers to form a hybrid enyme.

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