Enzymes are proteins that speed up chemical reactions. They are catalyst. Without catalyst, chemical reactions would still take place, but at a slower rate and the body wouldn’t benefit. All enzymes possess two essential properties. First, enzymes accelerate the rate of chemical reactions without being consumed and/or changed by the reaction. Second, enzymes accelerate reaction rates without changing the chemical equilibrium among reactants and products. Each enzyme has a receptor site, and they are very specific to which molecule (substrate) it will interact with. When a substrate is captured, it will either be combined to create a product or it will be broke down. Fructose is primarily metabolized in the liver. Fructose alone cannot be used as energy. It has to be broke down for use. Enzymes in the liver aid fructose metabolism. Fructose binds to the receptor site on the enzyme fructokinase. This enzyme uses ATP and ADP cycle (energy) to speed up the chemical reaction to convert fructose into Fru-1-p. Next, Fru-1-p will undergo the next reaction and will produce either DHAP or glyceraldehyde by way of the enzyme Aldolase B. (Wikipedia, 2015)
As stated above, Aldolase B is active specific to the substrate Fructose-1-Phosphate. Fructose-1-phos is derived from fructose. It’s produced by fructokinase which is available in the liver. It’s converted by aldolase B into dihydroxyacetone phosphate and glyceraldehyde. A deficiency in this enzyme (Aldolase B) caused a disorder called Hereditary Fructose Intolerance. This is a genetic mutation of chromosome 9 which is an autosomal recessive disorder, meaning that the trait must be passed from both parents. The mutation in Adolab gene results in hereditary fructose intolerance (HFI). Aldolab is accountable for creation of the Aldolase B enzyme. A deficiency in enzyme
