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Chapter 12 Regulation of Enzyme Activity;Outline;
;slow response time
energetically expensive
maximum activity limited only by relative rates for protein synthesis and degradation
generally used for long term changes in enzyme activity;Regulation of enzyme levels requires either an increase in the synthesis of the enzyme, or a decrease in the rate of its degradation (or the rate of the degradation of the mRNA that encodes the enzyme). Increasing protein synthesis is an expensive proposition, it takes 4 ATPs just to form one peptide bond. That’s 1 200 ATPs for one 300 amino acid protein!;Change of enzyme quality -Regulation of enzyme activity;Because regulation of enzyme activity does not usually involve protein synthesis, the amount of energy necessary is relatively small compared to other cellular functions. The notable exception to this general rule is regulation by protein inhibitors, which generally bind very tightly to their enzyme targets and must be digested to be removed.;Isozymes are physically distinct forms of the same enzyme.
Isozymes may differ from each other by differences in their amino acid sequences or by the presence of different posttranslational modifications in each isozyme.
The relative abundance of different isozymes varies for different tissues. The ability to control which isozymes are expressed in a particular cell allows each cell to adjust the enzyme activity based on the specific conditions that exist in the cell.;Quality control can be achieved by five different mechanisms;Allosteric = “other site” other than active site
Regulatory molecules called, effectors, modulators,regulatory molecules
Homotropic regulation: regulation by substrate at active site
Heterotropic regulation: regulation by molecule NOT substrate ( end products), at allosteric site
Few enzymes are allosteric
Allosteric enzymes DO NOT exhibit M-M kinetics;Physiology of allosteric enzymes;Allosteric regulators do not bind to the active site of the enzyme;Alloster
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