Galactosemia, an Inborn Error of Metabolism
Galactosemia
Galactosemia is an inborn error of metabolism. Because of energy barriers, essentially none of the chemical reactions that take place in living things could occur at any measurable rate without the presence of a catalyst. Most catalysts in living things are enzymes that depend on their structure to be able to function. Their structure is determined by their coding on DNA. Inborn errors of metabolism, like the one seen in galactosemia, are caused by defective genes. Galactosemia is an inherited metabolic disorder in which the transformation of galactose to glucose is blocked, allowing galactose to increase to toxic levels in the body (Chung 1997). Galactose epimerase, the enzyme in the liver that is required to break down galactose, is deficient in galactosemia patients ("Galactosemia" 1995 and Wohlers, Christacos, and Harreman 1999). This enzyme works as a catalyst to speed up the breakdown of galactose. When there is a deficiency of this enzyme, the body cannot metabolize galactose as quickly as needed, causing a toxic buildup (Olendore, Jenyan, and Bayden 1999). This disease is inherited in an autosomal recessive manner, this means that galactosemia is only present in individuals with two defective copies of any one of the three genes that causes it (Chung 1997). These genes are the genes that code for the three enzymes, galactosemia-1-phosphate-uridyl transferase (GALT), galactokinase (GALK), and uridyl disphosphogalactose-4-epimerase (Olendore, Jenyan, and Bayden 1999). Although carriers have less than normal enzyme activity, carriers of the disease are unaware that they are carrying a defective gene since no symptoms are evident (Chung 1997). If two carriers of the same defective gene have children, the chance of their child getting galactosemia by having two copies of the same defective gene is 25% for each pregnancy (Elsas 1999). Every cell nucleus has two copies of each gene, therefore, if only one of the two copies is
Galactosemia is an inborn error of metabolism. Because of energy barriers, essentially none of the chemical reactions that take place in living things could occur at any measurable rate without the presence of a catalyst. Most catalysts in living things are enzymes that depend on their structure to be able to function. Their structure is determined by their coding on DNA. Inborn errors of metabolism, like the one seen in galactosemia, are caused by defective genes. Galactosemia is an inherited metabolic disorder in which the transformation of galactose to glucose is blocked, allowing galactose to increase to toxic levels in the body (Chung 1997). Galactose epimerase, the enzyme in the liver that is required to break down galactose, is deficient in galactosemia patients ("Galactosemia" 1995 and Wohlers, Christacos, and Harreman 1999). This enzyme works as a catalyst to speed up the breakdown of galactose. When there is a deficiency of this enzyme, the body cannot metabolize galactose as quickly as needed, causing a toxic buildup (Olendore, Jenyan, and Bayden 1999). This disease is inherited in an autosomal recessive manner, this means that galactosemia is only present in individuals with two defective copies of any one of the three genes that causes it (Chung 1997). These genes are the genes that code for the three enzymes, galactosemia-1-phosphate-uridyl transferase (GALT), galactokinase (GALK), and uridyl disphosphogalactose-4-epimerase (Olendore, Jenyan, and Bayden 1999). Although carriers have less than normal enzyme activity, carriers of the disease are unaware that they are carrying a defective gene since no symptoms are evident (Chung 1997). If two carriers of the same defective gene have children, the chance of their child getting galactosemia by having two copies of the same defective gene is 25% for each pregnancy (Elsas 1999). Every cell nucleus has two copies of each gene, therefore, if only one of the two copies is