Biochemistry 3380G Lecture Notes - Lecture 10: Aspartate Carbamoyltransferase, Protein Kinase, Anabolism

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In a living cell, molecules flow through each metabolic pathway at some rate called flux: flux = rate of conversion of a to e. Control of flux is achieved by altering enzymatic activity. G 0: reaction is near equilibrium, changes in concentration heavily influence extent of reaction (le chatelier"s principle) Example: a 10-step metabolic pathway: net g is negative, most reactions are reversible, between 1&2, 3&4, 10&11 are reversible. Ways to control the rate of a reaction: change amount of enzyme, transcription, translation, degradation, change concentration of substrate or product, change enzyme activity, allosteric regulation, covalent modification, association with regulatory protein. Example: aspartate transcarbamoylase: ctp binds, conformational change, active site is no longer accessible and enzyme becomes inactive, an example of feedback inhibition. Covalent modification: a chemical group (eg. phosphate) is covalently added to the protein, changes the conformation of the enzyme, affecting activity, the bound form can either make the enzyme active or make it inactive.

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