P5538
Phosphoglucose Isomerase from Bacillus stearothermophilus
lyophilized powder, 300-1,000 units/mg protein
Synonym(s):
D-Glucose-6-phosphate ketol-isomerase, PGI, Phosphosaccharomutase
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About This Item
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form
lyophilized powder
Quality Level
specific activity
300-1,000 units/mg protein
mol wt
189 kDa
composition
Protein, ≥60% biuret
storage temp.
−20°C
General description
The enzyme is part of the glycolytic pathway. Also, it is important in the industrial production of fructose 1,6-diphosphate (FDP) from glucose. The molecular mass is found to be approximately 189 kDa and it consists of four subunits, each with a molecular mass of approximately 50 kDa. Optimum pH is found to be between 9-10 and the isoelectric point is 4.2.
Application
Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. It is used in sugar assays to convert fructose to glucose. This product is from Bacillus stearothermophilus.
The enzyme from Sigma has been used in the determination of fructose 6-phosphate in a mutant strain of Rhizobium meliloti.
Biochem/physiol Actions
Phosphoglucose Isomerase fuctions as an isomerase, neuroleukin, autocrine motility factor, and a differentiation and maturation mediator.
Unit Definition
One unit will convert 1.0 μmole of D-fructose 6-phosphate to D-glucose 6-phosphate per min at pH 9.0 at 30 °C.
Physical form
lyophilized powder containing Tris buffer
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
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)
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A Arias et al.
Journal of bacteriology, 137(1), 409-414 (1979-01-01)
A mutant strain of complex phenotype was selected in Rhizobium meliloti after nitrosoguanidine mutagenesis. It failed to grow on mannitol, sorbitol, fructose, mannose, ribose, arabitol, or xylose, but grew on glucose, maltose, gluconate, L-arabinose, and many other carbohydrates. Assay showed
The Kinetics and Mechanism of a Reaction Catalyzed by Bacillus stearothermophilus Phosphoglucose Isomerase.
Widjaja A, et al.
Journal of Fermentation and Bioengineering, 86(3), 324-331 (1998)
Veera Kainulainen et al.
Journal of bacteriology, 194(10), 2509-2519 (2012-03-06)
Glutamine synthetase (GS) and glucose-6-phosphate isomerase (GPI) were identified as novel adhesive moonlighting proteins of Lactobacillus crispatus ST1. Both proteins were bound onto the bacterial surface at acidic pHs, whereas a suspension of the cells to pH 8 caused their
Monica Totir et al.
PloS one, 7(2), e32498-e32498 (2012-03-07)
Structural biology and structural genomics projects routinely rely on recombinantly expressed proteins, but many proteins and complexes are difficult to obtain by this approach. We investigated native source proteins for high-throughput protein crystallography applications. The Escherichia coli proteome was fractionated
Simone Frédérique Brenière et al.
PLoS neglected tropical diseases, 6(5), e1650-e1650 (2012-06-12)
The current persistence of Triatoma infestans (one of the main vectors of Chagas disease) in some domestic areas could be related to re-colonization by wild populations which are increasingly reported. However, the infection rate and the genetic characterization of the
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