PGAM2 Lysate – Tissue Lysate

Phosphoglycerate mutase (PGAM) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. The PGAM is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). This gene encodes muscle-specific PGAM subunit. Mutations in this gene cause muscle phosphoglycerate mutase eficiency, also known as glycogen storage disease X. [provided by RefSeq, Sep 2009]

PGAM2: Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity. Defects in PGAM2 are the cause of glycogen storage disease type 10 (GSD10). A metabolic disorder characterized by myoglobinuria, increased serum creatine kinase levels, decreased phosphoglycerate mutase activity, myalgia, muscle pain, muscle cramps and excercise intolerance. Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily.

Protein type: Carbohydrate Metabolism - glycolysis and gluconeogenesis; Phosphatase (non-protein); Isomerase; EC 5.4.2.11; EC 5.4.2.4; EC 3.1.3.13

Chromosomal Location of Human Ortholog: 7p13-p12

Cellular Component: nucleus; cytosol

Molecular Function: phosphoglycerate mutase activity; bisphosphoglycerate mutase activity; bisphosphoglycerate phosphatase activity; cofactor binding; 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Biological Process: response to mercury ion; striated muscle contraction; glycolysis; dephosphorylation; carbohydrate metabolic process; glucose metabolic process; pathogenesis; spermatogenesis; gluconeogenesis

Disease: Glycogen Storage Disease X