Wednesday, April 24, 2019

Discuss lock-and-key theory of enzyme-substrate interaction giving Essay

Discuss lock-and-key theory of enzyme- substrate interaction bragging(a) specific example to illustrate theory. Include the effects of substrate closeness, pH cha - Essay ExampleEnzymes impart active sites which interact with the substrate. The structure of the active site is unique for that respective substrate. Just as a uniquely shaped key will only fit in to and open a interconnected lock, so it is with enzymes and their substrates. The wrong key may fit in to the lock, but nothing can run into because the match of shapes is not correct. This fit is so specific that the change in a single atomic number 1 atom in a molecule makes it lose its specificity to a particular enzyme. This means that it may not bind to the specific site and even if it does, the enzyme will be unable to do anything chemically to it. The substrate always fits into the enzymes active site and the active site is always a fold or incise in the enzyme. Enzymes are always larger than the substrate and the y are flexible so that they can turn tail and fold around the substrate (Refer to Figure.1). This is facilitated by the weak bonds that hold the enzyme in its functional shape. The union in the midst of an enzyme and its substrate is called the enzyme -substrate interlocking. When a substrate is bound to the active site, particular chemical bonds of the substrate are thinned and the substrate bends. This lowers the activating energy to the point where the heat in the environment is sufficient to supply the activation energy to initiate the reaction (Chapter 7, Metabolism and Biochemistry).If the amount of the enzyme is kept constant and the substrate concentration is because gradually increased, the reaction velocity will increase until it reaches a maximum. After this point, increases in substrate concentration will not increase the velocity. This means that when this maximum velocity had been reached, all of the available enzyme has been converted to the enzyme-substrate com plex (Refer to Figure.3).Michaelis developed a set of mathematical expressions to

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