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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:
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

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P1506G4509F0137
Pyruvate Kinase from rabbit muscle Type II, ammonium sulfate suspension, 350-600 units/mg protein

P1506

Pyruvate Kinase from rabbit muscle

Sigma-Aldrich

G4509

Glycerokinase from Escherichia coli

specific activity

100-300 units/mg protein

specific activity

350-600 units/mg protein

specific activity

40-100 units/mg protein

specific activity

≥50 units/mg protein

form

lyophilized powder

form

ammonium sulfate suspension

form

lyophilized powder

form

lyophilized powder

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

type

Type VIII

type

Type II

type

-

type

Type VII

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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.
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
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)
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)
Nicolas Galazis et al.
European journal of endocrinology, 168(2), R33-R43 (2012-10-25)
Women with polycystic ovary syndrome (PCOS) are at increased risk of developing insulin resistance and type 2 diabetes mellitus (T2DM). In this study, we attempted to list the proteomic biomarkers of PCOS and T2DM that have been published in the

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