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Published bySimon Whitehead Modified over 8 years ago
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Chapter 8.1, 8.2, 8.4, 8.5
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metabolism is the process of breaking down and creating molecules necessary for life ◦ each step in this process is driven by an enzyme which directs the speed of the reaction (enzymes are proteins!) catabolic--breakdown molecules cellular respiration anabolic--build molecules protein synthesis
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energy is the capacity to cause change ◦ kinetic (heat) vs. potential (chemical) thermodynamics = energy transformations ◦ 1st law (matter cannot be created or destroyed, only change form) ◦ 2nd law (energy transfer increases the entropy of the universe) spontaneous reactions vs. reactions that need energy
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free energy--identifies if a reaction requires energy to proceed ◦ higher free energy = unstable does not require outside energy for the reaction to happen (spontaneous) exergonic reaction (negative delta G) does not imply that it happens fast! ◦ lower free energy = stable requires outside energy for the reaction to proceed (nonspontaneous) endergonic reaction (positive delta G)
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Lower energy barriers for the reaction to happen at an increased rate (catalyst); not used up during the reaction ◦ activation energy (energy required to get reaction going) based on how difficult it is to break the chemical bonds ◦ speed up reactions that would occur anyway
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substrate (reactant an enzyme acts on) ◦ enzyme binds to substrate, forming enzyme- substrate complex ◦ each enzyme has a specific substrate (results from unique sequence of amino acids) active site (region of enzyme where substrate binds) ◦ when this occurs, the shape of the enzyme changes which enhances the reaction
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Rate in which enzyme converts substrate to product is determined by... ◦ the initial concentration of the substrate (or enzyme) more substrate molecules that are available the more frequently they access active site. limited by the enzyme concentration (saturated when rate of reaction is determined by how often substrate can move into active site) ◦ general environmental factors temperature, pH, and other chemicals each enzyme has optimal environment depending on the organism and where it needs to work
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competitive inhibition ◦ reduce the productivity of enzymes by blocking substrate from entering active site ◦ overcome by increasing concentration of substrate noncompetitive inhibition ◦ impede reactions by binding to another part of the enzyme, thus changing the shape of the active site and making it less effective ◦ **often pesticides, antibiotics, and toxins are inhibitors
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enzymes need to be told when and where to be active so only necessary reactions are occurring ◦ Allosteric regulation protein function changed by binding of another molecule has active (activator binds) and inactive (inhibitor binds) forms “Chemical on/off switch” ◦ feedback inhibition end product of reaction binds to enzyme causing inhibition, thus slowing the reaction down
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