Biochemistry 3381A Chapter Notes - Chapter 14: Protein Phosphatase, Zymogen, Alpha Helix

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Ways to regulate activity: increase/decrease number of enzyme molecules, increase/decrease activity of each enzyme molecule. The availability of substrates and cofactors usually determines how fast the reaction goes. Enzymes have evolved such that their km values approximate the prevailing in vivo concentration of their substrates: recall: km is substrate concentration that allows the enzyme to reach half vmax. As product accumulates, the apparent rate of the enzymatic reaction decreases. Enzymatic rate, v=d[p]/dt, slows down as product accumulates and equilibrium is approached. Apparent decrease due to conversion of p to s by the reverse reaction as [p] rises. Once [p]/[s] = keq, no further reaction is apparent: keq defines thermodynamic equilibrium. Product inhibition: some enzymes are inhibited by the products of their action. Genetic regulation of enzyme synthesis and decay determines the amount of enzyme present at any. Amounts of enzyme synthesized by cell determined by transcription regulation.

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