Enzyme Lock And Key Structure

As globular proteins, enzymes have a specific three-dimensional shape which is determined by their sequence of amino acids. This specific tertiary structure is held together by ionic bonds, hydrogen bonds and disulphide bridges. Despite their generally large size, enzyme molecules have a small region that is functional, known as; the active site. The substrate molecule is held within the active site by bonds that temporarily form between the R groups of the amino acids of the active site and groups on the substrate molecule. The enzyme is then able to break the bonds holding the substrate together, and so , making the substrate molecule break apart into several smaller molecules known as ‘products’. This structure is known as the enzyme-substrate

In other words, it is flexible and moulds itself around the substrate, just as a glove moulds itself to the shape of someone’s hand. The amino acid side chains of the enzyme can move into very precise positions to allow interaction with the substrate. As the enzyme alters its shape, the enzyme puts strain on the substrate molecule and thereby lowers its activation energy, this process is known as the induced fit theory of enzyme action.
Lipase is a type of enzyme known as a hydrolase and is responsible for catalysing the hydrolysis of triglycerides
(the substrate) into fatty acids and glycerol. It is referred to as a hydrolase because the reaction that it catalyses is a hydrolysis reaction – a reaction in which large molecules are broken down into smaller ones with the addition of water.
The molecules being broken down by lipase are lipids. Lipids are organic, non-polar compounds composed of carbon, hydrogen and oxygen which can be extracted using non-polar solvents such as alcohol and