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P1903

Sigma-Aldrich

Pyruvate Kinase from Bacillus stearothermophilus

Type VIII, lyophilized powder, 100-300 units/mg protein

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Synonym(s):
ATP:pyruvate 2-O-phosphotransferase, PK
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

Bacillus sp. (B. stearothermophilus)

Quality Level

type

Type VIII

form

lyophilized powder

specific activity

100-300 units/mg protein

storage temp.

2-8°C

Application

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.

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

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

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)
Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus
Suzuki, K.
Acta Crystallographica Section B, Structural Crystallography and Crystal Chemistry, F61, 759-761 (2005)
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
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)
Daniel I Benjamin et al.
Cell metabolism, 16(5), 565-577 (2012-10-16)
Cancer cells possess fundamentally altered metabolism that provides a foundation to support tumorigenicity and malignancy. Our understanding of the biochemical underpinnings of cancer has benefited from the integrated utilization of large-scale profiling platforms (e.g., genomics, proteomics, and metabolomics), which, together

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