PGAM2
PGAM2, also known as phosphoglycerate mutase 2 or PGAM-M, is the muscle-specific subunit of phosphoglycerate mutase. It catalyses the interconversion of 3-phosphoglycerate and 2-phosphoglycerate, a step in the glycolytic pathway. Browse Assay Genie's current range of PGAM2 research reagents below, or read on for the biology behind the target.
PGAM2 catalyses the interconversion of 3- and 2-phosphoglycerate, using 2,3-bisphosphoglycerate as the primer of the reaction. This is the reversible 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) reaction of the glycolytic pathway. The enzyme can also catalyse the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate, although with reduced activity. Two EC numbers, 5.4.2.11 and 5.4.2.4, reflect these activities.
Phosphoglycerate mutase is a dimeric enzyme. Different tissues contain different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme and a hybrid MB form. The PGAM2 gene encodes the muscle-specific subunit, which is why the protein is also called PGAM-M. PGAM2 belongs to the phosphoglycerate mutase family and the BPG-dependent PGAM subfamily. HGNC places it in the phosphoglycerate mutases and bisphosphoglycerate phosphatases gene groups. Mouse and rat both have a Pgam2 ortholog.
The previous HGNC name for the gene was phosphoglycerate mutase 2 (muscle). Mutations in the gene cause muscle phosphoglycerate mutase deficiency, also known as glycogen storage disease X. This makes PGAM2 a useful subject for studies of muscle glycolysis and inherited disorders of glycogen and glucose metabolism. Related isozyme subunits include PGAM1 (the brain-type subunit gene) and the distinct family member PGAM5.
PGAM2 catalyses the 3-phosphoglycerate to 2-phosphoglycerate step of glycolysis, making it relevant to studies of glycolytic flux.
As the muscle-specific subunit, PGAM2 helps define the MM and MB isozyme composition of phosphoglycerate mutase in muscle tissue.
Mutations in PGAM2 cause muscle phosphoglycerate mutase deficiency, also called glycogen storage disease X.
The MM, MB and BB dimer forms allow comparison of tissue-specific phosphoglycerate mutase isozymes and their catalytic activities.
PGAM2 catalyses the interconversion of 3- and 2-phosphoglycerate, with 2,3-bisphosphoglycerate as the primer, in the glycolytic pathway. It can also interconvert (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate, but with reduced activity. It encodes the muscle-specific subunit of phosphoglycerate mutase.
PGAM2 is the HGNC symbol for phosphoglycerate mutase 2. The alias is PGAM-M, for the muscle subunit, and the previous name was phosphoglycerate mutase 2 (muscle). The active enzyme is a dimer that forms MM, MB or BB isozymes depending on the tissue.
Mutations in PGAM2 cause muscle phosphoglycerate mutase deficiency, also known as glycogen storage disease X. Mouse and rat each have an ortholog named Pgam2. Check the datasheet of any product for its validated reactivity.
Other phosphoglycerate mutase family members and related glycolytic enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P15259; product specifications from Assay Genie datasheets.