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An enzyme alters the activation energy of a reaction Enzyme is AD – allows it to associate with substrate (molecule that will go thru reaction) Enzyme brings two substrates together in correct orientation (dehydration synthesis) or stresses bonds of substrate (hydrolysis) – lowers activation energy for new bonds to be formed/ broken Different types of cells have different types of enzymes – affects structure/function of cell Implication: Enzymes are vital for living things in that it peed up reactions that, if a catalyst weren’t present, would not be able to occur fast enough. . Concept: Active sites of enzymes conform to fit the shape of substrates Active site: place where substrate bind Binding of substrate causes enzyme to slightly change shape – induced fit Allows other substrates to bind with enzyme Implication: nothing really that important to be honest 3.
Concept: Environmental and other factors affect enzyme function Temperature Increase of temp causes unconcealed reaction to be faster due to more kinetic energy f reactants HOWEVER: catcalled reactions have an optimal temperature Increase of temp below the opt temp will increase reaction rates HOWEVER: once temperatures rises above opt temp, enzyme begins to break down (denature) Implication: Enzymes have different optimum temperatures, depending on the type of organism.
Human enzymes opt temp is about 35 Celsius while Prokaryote in hot springs have opt temp of 70 Celsius Ph Ionic interactions between charged amino acids also hold enzymes together These interactions are sensitive to [H+] BC. Hanging concentration CHANGES THE BALANCE teen negative and positively charged amino acids – therefore affects shape since these interactions hold enzyme together Most enzymes pH range = 6-8 Some enzymes can maintain AD shape even in extremely acidic/basic environment Pepsin has an optimal pH of 2, which is found in stomach acid Implication: Enzymes also have optimal pH values, depending on how well they can maintain shape in certain concentrations of hydrogen ion Inhibitors and activators Inhibitor: substrate that decreases an enzyme’s activity Competitive inhibitor: compete with substrate for same active site Noncompetitive inhibitor: bind to another place (NOT ACTIVE SITE NOR ALLEGORIC SITE) which changes shape of enzyme – unable to bind with substrate Allegoric enzyme: can be active or inactively configure Noncompetitive inhibitors (allegoric inhibitor) bind to allegoric site (site where switches enzyme on and of There are also allegoric activators (turn enzymes on) Implication: Through inhibitors/activators, cell can regulate activity of enzymes and therefore can be more efficient.
Enzyme cofactors Enzymes can be assisted by cofactors (usually metal ions in active site) Ex. Zinc ion is used in some enzymes to draw electrons away from bonds, making them less stable and easier to break Commence: cofactor that is a nonprofit, organic molecule (usually called vitamins) Ex. Vitamin B, modified nucleotides Consumes serve as electron acceptors (as implied above) – pass e- to other enzymes, which sometimes pair with protein to form hydrogen atom: consumes shuttle energy to other enzymes thru hydrogen atoms Implication: Cofactors are another factor that affects enzymatic function. Used to speed up reaction by making bonds less stable.