Pyruvate Kinase: Difference between revisions
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<StructureSection load='2vgb' size='350' side='right' scene='' caption='Human pyruvate kinase tetramer complex with fructose diphosphate, phosphoglycolic acid, Mn+2 and K+ (purple) ions (PDB code [[2vgb]])'> | |||
[[Pyruvate Kinase]] is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>. See [[Glycolysis Enzymes]]. | [[Pyruvate Kinase]] is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis; thereby, generating the second ATP of glycolysis and pyruvate. It is able to catalyze this step by transferring the phosphate group from phosphoenolpyruvate (PEP) to ADP <ref>{{book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=501|}}</ref>. See [[Glycolysis Enzymes]]. | ||
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Red blood cells, in a state of pyruvate kinase deficiency, rapidly become deficient in ATP and can undergo hemolysis.This is transmitted as an autosomal recessive trit. The severity of hemolysis is extremely variable such as a mild case to life-threatening neonatal anaemia requiring transfusions. Over one hundred eighty different mutations have been discovered in relation to this deficiency with most being autosomal recessive, but a few strands are autosomal dominant. The deficiency causes red blood cells to deform into echinocytes on peripheral blood smears. This causes the buildup of reaction intermediates which can also increase the level of 2,3-bisphosphoglycerate in the cells. This causes a rightward shift in the hemoglobin oxygen saturation curve, which means that there is a decreased oxygen affinity for the hemoglobin and earlier oxygen unloading than under normal conditions | Red blood cells, in a state of pyruvate kinase deficiency, rapidly become deficient in ATP and can undergo hemolysis.This is transmitted as an autosomal recessive trit. The severity of hemolysis is extremely variable such as a mild case to life-threatening neonatal anaemia requiring transfusions. Over one hundred eighty different mutations have been discovered in relation to this deficiency with most being autosomal recessive, but a few strands are autosomal dominant. The deficiency causes red blood cells to deform into echinocytes on peripheral blood smears. This causes the buildup of reaction intermediates which can also increase the level of 2,3-bisphosphoglycerate in the cells. This causes a rightward shift in the hemoglobin oxygen saturation curve, which means that there is a decreased oxygen affinity for the hemoglobin and earlier oxygen unloading than under normal conditions | ||
<ref>PMID:17360088</ref>. | <ref>PMID:17360088</ref>. | ||
</StructureSection> | |||
==3D structures of pyruvate kinase== | ==3D structures of pyruvate kinase== | ||
