P1903
Pyruvate Kinase from Bacillus stearothermophilus
Type VIII, lyophilized powder, 100-300 units/mg protein
Synonym(s):
ATP:pyruvate 2-O-phosphotransferase, PK
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About This Item
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biological source
Bacillus sp. (B. stearothermophilus)
type
Type VIII
form
lyophilized powder
specific activity
100-300 units/mg protein
storage temp.
2-8°C
General description
Research Area: CELL SIGNALING
Mammalian pyruvate kinase is a tetrameric protein composed of identical subunits organized in a dimer-of-dimers configuration. Four isoforms of pyruvate kinase exist in mammals, namely PKM1, PKM2, PKR, and PKL. Pyruvate kinase can be found in both tetrameric and dimeric forms.
Mammalian pyruvate kinase is a tetrameric protein composed of identical subunits organized in a dimer-of-dimers configuration. Four isoforms of pyruvate kinase exist in mammals, namely PKM1, PKM2, PKR, and PKL. Pyruvate kinase can be found in both tetrameric and dimeric forms.
Application
Pyruvate Kinase from Bacillus stearothermophilus may be used in biofuel production.
Pyruvate kinase from Bacillus stearothermophilus has been used in a study to assess evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon. It has also been used in a study to investigate the importance of the Lys221 active site for pyruvate kinase activity.
Biochem/physiol Actions
Pyruvate Kinase from Bacillus stearothermophilus is activated by AMP and ribose 5-phosphate.
Pyruvate kinase is an enzyme that facilitates the conversion of phosphoenolpyruvate (PEP) and ADP to pyruvate and ATP in glycolysis and is involved in the regulation of cell metabolism. It serves as a terminal enzyme in the glycolytic pathway. This reaction is favorable due to the high energy of hydrolysis of PEP.
Pyruvate kinase is a key regulator controlling metabolic flux and ATP production in glycolysis and is considered a potential drug target. Additionally, pyruvate kinases are subject to regulation by heterotropic effectors, with fructose 1,6-bisphosphate (FBP) being the most widely known allosteric activator of bacterial, yeast, and mammalian enzymes. Furthermore, PKM2, one of the four isoforms of pyruvate kinase, is extensively expressed in various types of tumors and is associated with tumorigenesis.
Pyruvate kinase is a key regulator controlling metabolic flux and ATP production in glycolysis and is considered a potential drug target. Additionally, pyruvate kinases are subject to regulation by heterotropic effectors, with fructose 1,6-bisphosphate (FBP) being the most widely known allosteric activator of bacterial, yeast, and mammalian enzymes. Furthermore, PKM2, one of the four isoforms of pyruvate kinase, is extensively expressed in various types of tumors and is associated with tumorigenesis.
Unit Definition
One unit will convert 1.0 μmole of phospho(enol)pyruvate to pyruvate per min at pH 7.2 at 30 °C.
Physical form
Lyophilized powder containing Tris buffer salts, pH 8.5
Analysis Note
Protein determined by biuret
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon
Sakai, H. and T. Ohta
FEBS Journal, 211, 851-859 (1993)
E W Walters et al.
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Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus
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Acta Crystallographica Section B, Structural Crystallography and Crystal Chemistry, F61, 759-761 (2005)
An overview of structure, function, and regulation of pyruvate kinases
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Protein Science, 28(10), 1771-1784 (2019)
Mutagenesis of the active site lysine 221 of the pyruvate kinase from Bacillus stearothermophilus
Sakai, H.
The Journal of Biological Chemistry, 137, 141-145 (2005)
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