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P1903

Sigma-Aldrich

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

CAS Number:
9001-59-6
Enzyme Commission number:
2.7.1.40 (BRENDA, IUBMB)
EC Number:
232-616-2
MDL number:
MFCD00081946
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

Bacillus sp. (B. stearothermophilus)

Quality Level

200

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.

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.

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

P1903-100UN:
P1903-500UN:
P1903-2.5KU:
P1903-VAR:
P1903-BULK:
P1903-1KU:

Certificates of Analysis (COA)

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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)
Protein kinase function of pyruvate kinase M2 and cancer
Chen X, et al.
Cancer Cell International, 20(1), 523-523 (2020)
E W Walters et al.
Plant physiology, 114(2), 549-555 (1997-06-01)
Adenylosuccinate synthetase (AdSS) is the site of action hydantocidin, a potent microbial phytotoxin. A kinetic analysis of the mode of inhibition of a plant adenylosuccinate synthetase by the active metabolite 5'-phosphohydantocidin (5'-PH) was the objective of the present study. AdSS
An overview of structure, function, and regulation of pyruvate kinases
Schormann N, et al.
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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