|Related Categories||2.7.x.x Phosphorus containing groups, 2.x.x.x Transferases, Application Index, Biochemicals and Reagents, Cell Biology,|
|form||buffered aqueous glycerol solution|
|foreign activity||lactic dehydrogenase and creatine phosphokinase ≤0.01%|
|phosphoglucomutase and myokinase ≤0.05%|
Protein determined by biuret.
One unit will convert 1.0 μmole of phospho(enol)pyruvate to pyruvate per min at pH 7.6 at 37 °C.
Solution in 50% glycerol containing 0.01 M phosphate, pH 7.0
Pyruvate kinase is an enzyme involved in glycolysis and is involved in gluconeogenesis. Product P7768 is from rabbit muscle and is provided in a buffered aqueous glycerol solution and has been used in PGM enzyme assays to determine phosphoglycerate mutase activity1. Pyruvate kinase is also used to study pyruvate kinase (PK) deficiency2.
Molecular Weight: 237 kDa and exists as a tetramer of four equal subunits of molecular weight 57 kDa.
Isoelectric Point: 7.6
Optimal pH: ∼7.5
Optimal Temperature: 25°C
ΕA280 = 0.54 for 1 mg(p)/ml, 1 cm path
Reported KM values are ATP (0.86 mM), pyruvate (10 mM), ADP (0.3 mM), and PEP (0.07 mM) in Tris buffer at pH 7.4 and 30 °C. Pyruvate kinase is highly specific for phosphoenolpyruvate, but can utilize other dinucleotide triphosphates as substrates in place of ATP including GTP, ITP, dATP, UTP, and CTP.
Pyruvate kinase catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP. This transfer yields one molecule of pyruvate and one molecule of ATP. Molecular Weight: 237 kDa and exists as a tetramer of four equal subunits of molecular weight 57 kDa.
Isoelectric Point: 7.6
Optimal pH: ∼7.5
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buffered aqueous glycerol solution, 900-1400 units/mL lactic dehydrogenase, 600-1,000 units/mL pyruvate kinase
Certificate of Analysis
Certificate of Origin
|Personal Protective Equipment||Eyeshields, Gloves, half-mask respirator (US), multi-purpose combination respirator cartridge (US)|
From our library of Related Content, Sigma-Aldrich presents Enzyme Explorer: the most comprehensive source of enzymes, substrates, activators, & inhibitors.
Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
1. Cofactor-independent Phosphoglycerate Mutase Has an Essential Role in Caenorhabditis elegans and Is Conserved in Parasitic Nematodes Yinhua Zhang, Jeremy M. Foster, et al. J. Biol. Chem. 279, 37185-37190, (2004)
2. Studies on Pyruvate Kinase (PK) Deficiency: II. Electrophoretic, Kinetic, and Immunological Studies on Pyruvate Kinase of Erythrocytes and Other Tissues Kiichi IMAMURA, Takehiko TANAKA, et al. J. Biochem. 74, 1165-1175, (1973)
Pyruvate kinase deficiency in sub-Saharan Africa: identification of a highly frequent missense mutation (G829A;Glu277Lys) and association with malaria. Machado P, Manco L, Gomes C, et al. PLoS ONE 7(10), e47071, (2012)
Analysis of energy generation and glycolysis pathway in diminazene aceturate-resistant Babesia gibsoni isolate in vitro. Rajapakshage BK, Yamasaki M, Murakami M, et al. Jpn. J. Vet. Res. 60(2-3), 51-61, (2012)
Identification of regions of rabbit muscle pyruvate kinase important for allosteric regulation by phenylalanine, detected by H/D exchange mass spectrometry. Prasannan CB, Villar MT, Artigues A, et al. Biochemistry 52(11), 1998-2006, (2013)
Farnesoid X receptor inhibits the transcriptional activity of carbohydrate response element binding protein in human hepatocytes. Caron S, Huaman Samanez C, Dehondt H, et al. Mol. Cell. Biol. 33(11), 2202-11, (2013)
G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Beutler E, Westwood B, van Zwieten R, et al. Hum. Mutat. 9(3), 282-5, (1997)
Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Williams JM, Chen GC, Zhu L, et al. Mol. Microbiol. 27(1), 171-86, (1998)
Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Kanno H, Fujii H, Hirono A, et al. Blood 79(5), 1347-50, (1992)
cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Kanno H, Fujii H, Hirono A, et al. Proc. Natl. Acad. Sci. U. S. A. 88(18), 8218-21, (1991)
Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK. van Wijk R, Huizinga EG, van Wesel AC, et al. Hum. Mutat. 30(3), 446-53, (2009)
Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Kanno H, Fujii H, Tsujino G, et al. Biochem. Biophys. Res. Commun. 192(1), 46-52, (1993)
Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Kanno H, Fujii H, and Miwa S Blood 81(9), 2439-41, (1993)
Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Zarza R, Alvarez R, Pujades A, et al. Br. J. Haematol. 103(2), 377-82, (1998)
A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Cohen-Solal M, Préhu C, Wajcman H, et al. Br. J. Haematol. 103(4), 950-6, (1998)
An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate. Ashizawa K, McPhie P, Lin KH, et al. Biochemistry 30(29), 7105-11, (1991)
Complete genomic sequence of the human PK-L/R-gene includes four intragenic polymorphisms defining different haplotype backgrounds of normal and mutant PK-genes. Lenzner C, Nürnberg P, Jacobasch G, et al. DNA Seq. 8(1-2), 45-53, (1997)
Optimization and structure-activity relationships of a series of potent inhibitors of methicillin-resistant Staphylococcus aureus (MRSA) pyruvate kinase as novel antimicrobial agents. Kumar NS, Amandoron EA, Cherkasov A, et al. Bioorg. Med. Chem. 20(24), 7069-82, (2012)
Metabolic responses to iron deficiency in roots of Carrizo citrange [Citrus sinensis (L.) Osbeck. x Poncirus trifoliata (L.) Raf]. Martínez-Cuenca MR, Iglesias DJ, Talón M, et al. Tree Physiol. 33(3), 320-9, (2013)
Proteomic biomarkers of preterm birth risk in women with polycystic ovary syndrome (PCOS): a systematic review and biomarker database integration. Galazis N, Docheva N, Nicolaides KH, et al. PLoS ONE 8(1), e53801, (2013)
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