磷酸葡萄糖变位酶I来源于人，Phosphoglucomutase 1 human [PGM1]；lyophilized powder, recombinant, expressed in E. coli, ≥400 units/mg protein

Phosphoglucomutase-1 (PGM1) is an evolutionarily conserved enzyme[1] that belongs to the phosphohexose mutase family.[2] It is the major isoform of PGM in skeletal muscle and most other tissues.[3] The PGM1 gene is mapped to human chromosome 1p31.3.[4]

 

Phosphoglucomutase-1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P).[1] It regulates carbohydrate metabolism, energy production, and protein N-glycosylation.[2] PGM1 participates in the biosynthesis of nucleotide sugars required for glycan biosynthesis.[5] Variation in the PGM1 gene leads to PGM1 deficiency, which is considered an inherited metabolic disorder in humans.[2][5] PGM1 deficiency causes autosomal recessive diseases such as glycogen storage disease type XIV and congenital disorder of protein N-glycosylation.[5] 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.[1][6] PGM1 acts as a metabolic tumor suppressor.[4]

 

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.

 

Supplied as a lyophilized powder containing tris-buffered saline, EDTA, DTT and stabilizer.