Pyruvate Kinase: Difference between revisions
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[[Pyruvate Kinase]] is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis | [[Pyruvate Kinase]] is an enzyme that is involved in glycolysis. Pyruvate kinase’s function is to catalyze the last step of glycolysis, resulting in the formation of ATP 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>. | ||
{{STRUCTURE_2vgb | PDB=2vgb | SCENE= }} | {{STRUCTURE_2vgb | PDB=2vgb | SCENE= }} | ||
==Structure== | ==Structure== | ||
This | This protein structure is of pyruvate kinase from Homo sapiens and has the abbreviation PK. Pyruvate kinase belongs to the all beta proteins class and has the PK beta-barrel domain-like fold. It belongs to the PK beta-barrel domain-like superfamily and pyruvate kinase beta-barrel domain family<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>. | ||
Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the <scene name='Keegan_Gelvoria_Sandbox_1/Ligands/1'>K+</scene> and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>. | Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the <scene name='Keegan_Gelvoria_Sandbox_1/Ligands/1'>K+</scene> and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html|}}</ref>. | ||
