Enzyme Substrate Complex Lab Report

Structure:
Enzymes are globular proteins that act as catalysts, they have a specific 3D shape that is the result of their amino acid sequence. There is a specific region of the enzyme that is functional, this is called the active site. The active site is made up of a small number of amino acids and forms a small depression within the larger enzyme molecule. Moreover, the molecule that the enzyme acts upon (substrate) fits precisely into the depression and forms an enzyme-substrate complex. The substrate molecule is held into the active site by bonds that temporarily form between certain amino acids of the active site and groups on the substrate molecule.

Enzyme-substrate complex:
The enzyme-substrate complex formed when the enzyme binds with its substrate lowers the activation energy (minimum amount of energy needed to activate the
There are two models for enzyme action: the lock and key model and the induced fit model. The lock and key model asserted that the enzyme (the rigid lock) binds with the complementary substrate (the key). This model suggests that the enzyme and substrate fit perfectly together. This theory, however, has been corrected by the induced fit model as it has been observed that the active site of an enzyme changes shape when in the presence of a non-competitive inhibitor.
The induced fit model shows that an enzyme is flexible and can mould itself around the substrate. At the presence of a substrate, the shape of the enzyme is altered. The strain, caused by the enzyme changing shape in order to accommodate the substrate, distorts a bons in the substrate and lowers the activation energy needed to break bonds. This model proposes that enzymes are not rigid structures and can alter sightly when occupied by a