P5538
Phosphoglucose Isomerase from Bacillus stearothermophilus
lyophilized powder, 300-1,000 units/mg protein
Synonyme(s) :
D-Glucose-6-phosphate ketol-isomerase, PGI, Phosphosaccharomutase
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About This Item
Produits recommandés
Forme
lyophilized powder
Niveau de qualité
Activité spécifique
300-1,000 units/mg protein
Poids mol.
189 kDa
Composition
Protein, ≥60% biuret
Température de stockage
−20°C
Description générale
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.
Actions biochimiques/physiologiques
Phosphoglucose Isomerase fuctions as an isomerase, neuroleukin, autocrine motility factor, and a differentiation and maturation mediator.
Définition de l'unité
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.
Forme physique
lyophilized powder containing Tris buffer
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (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)
Natsuko Miura et al.
Eukaryotic cell, 11(8), 1075-1082 (2012-07-04)
Glycolytic enzymes are cytosolic proteins, but they also play important extracellular roles in cell-cell communication and infection. We used Saccharomyces cerevisiae to analyze the secretory pathway of some of these enzymes, including enolase, phosphoglucose isomerase, triose phosphate isomerase, and fructose
Sean D Schoville et al.
PloS one, 7(6), e40035-e40035 (2012-07-07)
The marine copepod Tigriopus californicus lives in intertidal rock pools along the Pacific coast, where it exhibits strong, temporally stable population genetic structure. Previous allozyme surveys have found high frequency private alleles among neighboring subpopulations, indicating that there is limited
Baiqing Wang et al.
Journal of molecular evolution, 74(1-2), 96-111 (2012-03-06)
Little is known of intron sequences' variation in cases where eukaryotic gene coding regions undergo strong balancing selection. Phosphoglucose isomerase, PGI, of Colias butterflies offers such a case. Its 11 introns include many point mutations, insertions, and deletions. This variation
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