Enzyme

Glucose-6-phosphate dehydrogenase deficiency (G6PD deficiency) is an X-linked recessive inborn error

of metabolism that predisposes to hemolysis and resultant jaundice in response to a number of triggers,
such as certain foods, illness, or medication. The condition is characterized by abnormally low levels
of glucose-6-phosphate dehydrogenase, an enzyme involved in the pentose phosphate pathway that is
especially important in the red blood cell. Carriers of the G6PD allele appear to be protected to some
extent against malaria

Prolonged Neonatal jaundice, possibly leading to kernicterus (arguably the most serious complication
of G6PD deficiency)
Hemolytic crises in response to:
Illness (especially infections)
Certain drugs : Antimalarial drugs that can cause acute hemolysis in people with G6PD deficiency
include primaquine, pamaquine,
Certain foods, most notably broad beans : Favism
Certain chemicals
Diabetic ketoacidosis
Very severe crises can cause acute kidney failure

G6PD Deficiency is a hereditary abnormality in the activity of an erythrocyte (red blood cell) enzyme. This
enzyme, glucose-6-phosphate dehydrogenase (G-6-PD), is essential for assuring a normal life span for red
blood cells, and for oxidizing processes. This enzyme deficiency may provoke the sudden destruction of
red blood cells and lead to hemolytic anemia with jaundice following the intake of fava beans, certain
legumes and various drugs.
Common symptoms of a hemolytic crisis include:
Sudden rise of body temperature and yellow coloring of skin and mucous membrane.

Dark yellow-orange urine.

Pallor, fatigue, general deterioration of physical conditions.

Heavy, fast breathing.

Weak, rapid pulse.

Many of these signs may occur when your baby eats foods, like fava beans, which contain chemicals that
cause the red blood cells to break down. They can also be triggered by certain drugs, illnesses, and
infections.

Pyruvate kinase deficiency, also called erythrocyte pyruvate kinase deficiency, is

an inherited metabolic disorder of the enzyme pyruvate kinase which affects the survival of red blood cells
Both autosomal dominant and recessive inheritance have been observed with the disorder; classically, and
more commonly, the inheritance is autosomal recessive.
Symptoms

Low count of healthy red blood cells (anemia)

Swelling of the spleen (splenomegaly)
Yellow color of the skin, mucous membranes, or white part of the eyes (jaundice)
Neurologic condition, called kernicterus, that affects the brain
Fatigue, lethargy
Pale skin (pallor)
In infants, not gaining weight and growing as expected (failure to thrive)
Gallstones, usually in the teens and older

Pyruvate kinase deficiency is due to mutation in PKLR gene, which makes enzyme pyruvate kinase. This
enzyme is important in glycolysis, this in turn causes a lesser amount of ATP in red blood cells.
The pathophysiology of pyruvate kinase deficiency has erythrocytes manufacture ATP through glycolysis. A
deficiency in pyruvate kinase, the enzyme that potentiates the last step of glycolysis
(phosphoenolpyruvate converted to pyruvate), results in red blood cells (RBCs) with decreased energy.
Because red blood cells cannot synthesize ATP, cellular death occurs, this is called a 'dehydration at
cellular level'. Due to the unavailability of adequate ATP, all active processes in the red blood cell comes
to a halt. Sodium potassium ATPase pumps are the first to stop, since the cell membrane is more
permeable to potassium than sodium, potassium leaks out. Inter cellular fluid becomes hypotonic, water
moves down its concentration gradient out of the cells. Finally cells shrink and die, the mechanism of how
distorted red blood cells are destroyed in the spleen is not understood. Sodium influx causes the cell to
become hypertonic. This results in an influx of water, causing cell rigidity, and eventually leading to
extravascularhemolysis.