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What are the optimum operating conditions for enzymes? - Coggle Diagram

- - - - The specific optimal pH level of an enzyme, where the rate of the enzyme's reaction is at maximum, is dependent on the type of enzyme and the location of where the enzyme is found. A change in pH with either too high or low pH will result in the enzyme's rate of reaction decreasing and change in the enzyme's 3D shape and thus a loss in enzyme activity. Majority of enzymes work between the pH range of 5-9 however, some enzymes are able to work in extremely acidic or basic pH levels(Creative Enzymes, 2023).
        
        An example would be pepsin; an enzyme that works in the stomach that breaks down proteins. The enzyme's optimum pH is 2.5 where it works in the pH range of 1-4 thus being very acidic. Contrastingly, the enzymes arginase have maximal activity in the pH range of 9-9.5 being extremely basic(The Journal of Nutrition, 2004).
    - - Different enzymes achieve the most activity at an specific temperature depending on where they are located. Most enzymes, specifically found within the human body/warm blooded animals, have an optimal temperature of 37°C. Enzymes within the human body tend to have an optimal temperature of 37°C due to the 37°C being the normal body temperature(Creative Enzymes, 2023). However, some enzyme's are able to work in higher/lower temperatures like enzyme's inside bacteria found in more thermal areas where they have a higher optimal temperature(BiteSizeBio, 2022).
    - - The process of changing the enzyme's 3D shape due to changes in temperature and pH can result in enzyme denaturation. Denaturation is the process at which the bonds within proteins are broken responsible for it's structure thus the active site of the enzyme is changed, reducing the ability of the substrates binding(Study.com, 2023).
- - - - What factors affect enzyme's reaction rates?
        
        Inhibitors; Inhibitors are molecules that bind to enzymes, either temporarily or permanently, to disrupt the compatibilty between the enzyme and substrate to thus slow down the enzyme/catalyst reaction. There are two maintypes of inhibitors; competitive and noncompetitive(Infinita,2021).
        
        Competitive inhibitors are molecules shaped similarily to substrate molecules, that specifically compete with the normal substrate for the active site position of the enzyme thus preventing the enzyme-substrate formation(Britannica, n.d). Due to this, less substrates bind to the enzyme's active site and thus the reaction rate of the enzyme decreases. However, competitive inhibitors only inhibit the active site temporarily and eventually leaves the enzyme. The level of inhibition of the active site depends on the concentration of the substrate and the inhibitor as they are competing(Sciencedirect, 2019).
        
        Non-competitive inhibitors are molecules that do not bind to the enzyme's acitve site and instead, bind to another site of the enyzme; the allosteric site. The inhibitor binding to the allosteric site affects the shape of the active site and thus the specific active site and the substrate cannot fit as well as before. Therefore, the normal rate of the pairing between the active site and the substrate is slowed down rather than stopped. As these inhibitors aren't competing with the substrates, the concentration of the substrate doesn't affect the inhibitor(Sciencedirect, 2019). Non-competitive inhibitors are irriversible and permanent due to the strong bonds between the inhibitor and the enzyme resulting in effectively denaturing the inhibited enzymes.(LibreTexts, 2022).
        
        Substrate concentration; An increase in the concentration of substrates within the enzyme will cause the the enzyme to become saturated with substrates, increasing the enzyme/catalyst reaction rate to a certain point. Due to more available substrates, the activity of the corresponding enzymes colliding with the substrate increases (Bioninja, n.d). After all enzymes are bound, the rate of reaction will not increase due to the enzyme's being saturated and working at their maximum rate(Khan academy, n.d).
        
        Enzyme concentration; An increase in the concentration of enzymes will increase the enzyme's reaction rate as the substrates have more availability in binding with the enzyme's active site(Creative Enzymes, 2023). After all substrates are bound, there is no longer any increase in the reaction rate as the enzyme can't bind with any substrates(Khan academy, n.d).F
        
        Temperature; The more increase in temperature, the more increased rate of enzyme reaction as the higher the temperature, the more energy for the collisions between the molecules(Khan academy, n.d). The point where the optimum temperature of the enzyme is passed will result in a decrease in enzyme activity as extreme high temperature will cause the enzyme to lose it's configuration and denature, thus stopping the enzyme from functioning. At low temperatures, enzyme-substrate collision activity decreases as their molecular movement is lowered thus the reaction is slower(BBC, 2023).
        
        pH; As every enzyme has a optimum pH, at this pH is the enzyme's fastest catalyst rate. Any change of the specific pH will cause the enzymatic reaction rate to decrease as the enzyme and substrate's shape is altered(Biologywise,n.d). Too high pH levels will cause the enzyme to denature(Khan academy, n.d).