Pyruvate Kinase: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
Line 2: Line 2:
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>.
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>.
{{STRUCTURE_2vgb |  PDB=2vgb  |  SCENE=  }}
{{STRUCTURE_2vgb |  PDB=2vgb  |  SCENE=  }}
==Structure==
This particular protein is found in 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>.


==Mechanism==
==Mechanism==
Line 9: Line 15:




==Structure==
This particular protein is found in 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>.


==Kinetics and Regulation==
==Kinetics and Regulation==