What does aldolase enzyme do?
Aldolase is a cytoplasmic enzyme involved in glucose and fructose metabolism. It specifically catalyzes the reversible reaction of converting fructose 1,6-bisphosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehydes 3-phosphate. The enzyme works on six reversible reactions in gluconeogensis and glycolysis.
What causes aldolase deficiency?
Fructose 1-phosphate aldolase deficiency or hereditary fructose intolerance (HFI) is an autosomal recessive disorder caused by the deficiency in aldolase B (fructose-1, 6-bisphosphate aldolase), an enzyme responsible for the cleavage of fructose-1-phosphate.
What does fructose-1-phosphate aldolase do?
h. Hereditary fructose intolerance is the result of a deficiency of the enzyme fructose-1-phosphate aldolase, which causes fructose-1-phosphate to accumulate in the liver. Fructose-1-phosphate is a competitive inhibitor of phosphorylase, an enzyme that regulates the conversion of glycogen to glucose.
What is aldolase deficiency?
Aldolase A deficiency, is an autosomal recessive metabolic disorder resulting in a deficiency of the enzyme aldolase A; the enzyme is found predominantly in red blood cells and muscle tissue.
What causes elevated aldolase?
Elevated aldolase is usually a sign of muscle or liver damage. For example, muscle damage from a heart attack releases aldolase in large quantities. Liver damage, such as hepatitis or cirrhosis, raises aldolase levels as well.
Why is aldolase test done?
Aldolase levels in the blood rise when a person has muscle damage. The aldolase blood test may be ordered to diagnose and monitor certain conditions related to skeletal muscle. It largely has been replaced by other muscle enzyme tests, especially CK (creatine kinase).
What is the aldolase blood test for?
What is another name for aldolase?
Aldolase A (ALDOA, or ALDA), also known as fructose-bisphosphate aldolase, is an enzyme that in humans is encoded by the ALDOA gene on chromosome 16.
What is a normal aldolase level?
Normal results range between 1.0 to 7.5 units per liter (0.02 to 0.13 microkat/L). There is a slight difference between men and women. Normal value ranges may vary slightly among different laboratories. Some labs use different measurements or test different samples.
What is considered a high aldolase level?
Generally, the normal range for adults is between 1.0 and 7.5 units per liter. The normal amount of aldolase in the blood is higher in children. For those under age 18, anything under 14.5 units per liter is considered normal.
Is aldolase reversible?
2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Glycolysis, a catabolic pathway, uses the forward reaction.
Why do they test for aldolase?
What happens if you have a deficiency of aldolase A?
Aldolase A deficiency, is an autosomal recessive metabolic disorder resulting in a deficiency of the enzyme aldolase A; the enzyme is found predominantly in red blood cells and muscle tissue. The deficiency may lead to hemolytic anaemia as well as myopathy associated with exercise intolerance and rhabdomyolysis in some cases.
Where are aldolase B enzymes found in the body?
Four identical aldolase B enzymes need to be attached (bound) to each other in a four-enzyme unit called a tetramer to work. Aldolase B is found primarily in the liver, but it is also present at lower levels in kidney and intestinal cells.
What causes elevated aldolase levels in the blood?
The aldolase test measures the amount of aldolase in your blood. Increased levels of this enzyme may indicate a serious health problem. Elevated aldolase is usually a sign of muscle or liver damage. For example, muscle damage from a heart attack releases aldolase in large quantities.
What kind of muscle pain does aldolase A cause?
Aldolase A deficiency is a rare, autosomal recessive disorder that is linked to hemolysis and accompanied by weakness, muscle pain, and myopathy.