SAE0022
Phosphoglucomutase 1 human
lyophilized powder, recombinant, expressed in E. coli
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About This Item
Produits recommandés
Produit recombinant
expressed in E. coli
Niveau de qualité
Description
PGM1 isoform sequence with a predicted molecular mass of 61.3kDa.
Pureté
≥95% (PAGE)
Forme
lyophilized powder
Activité spécifique
≥400 units/mg protein
Conditions d'expédition
dry ice
Température de stockage
−20°C
Description générale
Phosphoglucomutase-1 (PGM1) is an evolutionarily conserved enzyme that belongs to the phosphohexose mutase family. It is the major isoform of PGM in skeletal muscle and most other tissues. The PGM1 gene is mapped to human chromosome 1p31.3.
Actions biochimiques/physiologiques
Phosphoglucomutase-1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P). It regulates carbohydrate metabolism, energy production, and protein N-glycosylation. PGM1 participates in the biosynthesis of nucleotide sugars required for glycan biosynthesis. Variation in the PGM1 gene leads to PGM1 deficiency, which is considered an inherited metabolic disorder in humans. PGM1 deficiency causes autosomal recessive diseases such as glycogen storage disease type XIV and congenital disorder of protein N-glycosylation. Affected patients show multiple disease phenotypes, reflecting the central role of the enzyme in glucose homeostasis. The influence of PGM1 deficiency on protein glycosylation patterns is also widespread. PGM1 acts as a metabolic tumor suppressor.
Définition de l'unité
One unit will convert 1.0 μmole of α-D-Glucose-1-Phosphate to α-D-Glucose-6-phosphate per minute at pH 7.4 at 30 °C.
Forme physique
Supplied as a lyophilized powder containing tris-buffered saline, EDTA, DTT and stabilizer.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Wo-Tu Tian et al.
Neuromuscular disorders : NMD, 29(4), 282-289 (2019-02-10)
The congenital disorders of glycosylation are a group of clinically and biochemically heterogeneous diseases characterized by multisystem involvement due to glycosylation defect of protein and lipid. Here we report a 49-year-old man with exercise-induced fatigue and pain of muscle, tachypnea
Paul Hoff Backe et al.
Scientific reports, 10(1), 5656-5656 (2020-03-30)
Human phosphoglucomutase 1 (PGM1) is an evolutionary conserved enzyme that belongs to the ubiquitous and ancient α-D-phosphohexomutases, a large enzyme superfamily with members in all three domains of life. PGM1 catalyzes the bi-directional interconversion between α-D-glucose 1-phosphate (G1P) and α-D-glucose
Amichai Gutgold et al.
The Journal of clinical endocrinology and metabolism, 102(2), 345-349 (2016-10-19)
Hypoglycemia is a rare event in healthy adults, and the differential diagnosis includes many diseases, some of which are rare and easily missed. A 20-year-old male military paramedic was referred to our emergency department for investigation of recurrent hypoglycemia episodes
Eva Morava
Molecular genetics and metabolism, 112(4), 275-279 (2014-07-07)
We recently redefined phosphoglucomutase-1 deficiency not only as an enzyme defect, involved in normal glycogen metabolism, but also an inborn error of protein glycosylation. Phosphoglucomutase-1 is a key enzyme in glycolysis and glycogenesis by catalyzing in the bidirectional transfer of
Guang-Zhi Jin et al.
PLoS biology, 16(10), e2006483-e2006483 (2018-10-20)
Glycogen metabolism commonly altered in cancer is just beginning to be understood. Phosphoglucomutase 1 (PGM1), the first enzyme in glycogenesis that catalyzes the reversible conversion between glucose 1-phosphate (G-1-P) and glucose 6-phosphate (G-6-P), participates in both the breakdown and synthesis
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