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PGAM2 is the muscle-specific phosphoglycerate mutase isoform (PGAM-M), distinct from the brain-predominant PGAM1, consistent with the UniProt identity for P16290 and the muscle/heart bias of Pgam2 expression.
"Mammals express at least two major PGAM isoforms: **PGAM1 (Pgam1; often described as brain-predominant)** and **PGAM2 (Pgam2; muscle-specific)**"
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PGAM2 catalyzes the reversible interconversion of 3-phosphoglycerate and 2-phosphoglycerate in lower glycolysis, supporting the phosphoglycerate mutase activity and glycolysis annotations.
"PGAM2 is a **glycolytic enzyme** that catalyzes the **reversible isomerization of 3-phosphoglycerate (3-PG) to 2-phosphoglycerate (2-PG)** in the “lower” portion of glycolysis"
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The PGAM-family catalytic mechanism is a 2,3-bisphosphoglycerate-dependent phospho-histidine cycle, consistent with the BPG-dependent PGAM subfamily assignment and bisphosphoglycerate mutase activity.
"The canonical PGAM-family mechanism proceeds via a **phospho-histidine catalytic cycle**, commonly summarized as involving an **active-site histidine (often referred to as His11)** and a **2,3-bisphosphoglycerate (2,3-BPG/2,3-DPG)**-dependent priming/turnover mechanism"
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PGAM2 is a cytosolic enzyme; no evidence supports stable non-cytosolic localization, with the dominant functional context being intracellular carbohydrate metabolism.
"Within the provided evidence set, PGAM2 is described as a **cytosolic** enzyme in an isoform table summary"
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No support for stable extracellular or organellar localization of mammalian PGAM2; the dominant context is intracellular carbohydrate metabolism (argues against the ooplasm annotation).
"No evidence in the retrieved texts supports stable extracellular localization for mammalian PGAM2, and the dominant functional context is **intracellular carbohydrate metabolism**"
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PGAM2 is expressed mainly in skeletal muscle and heart, the basis for its muscle-context annotations (e.g. striated muscle contraction kept as non-core/over-annotation rather than core MF).
"PGAM2 is described as expressed mainly in **skeletal muscle and heart**"
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PGAM2 activity is regulated by SUMOylation at K49 and K176, which is functionally tied to myogenic differentiation (regulatory context, not a core catalytic annotation).
"PGAM2 is reported to undergo **SUMOylation**, with two primary SUMO acceptor lysines **K49 and K176**; mutating either lysine prevents SUMOylation"
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PGAM2 catalytic activity is gated by reversible acetylation at K100, with SIRT2-mediated deacetylation activating the enzyme under oxidative stress (regulatory context).
"PGAM2 activity is strongly regulated by lysine acetylation at **K100**: acetylation at K100 inhibits PGAM2 activity, whereas deacetylation activates it"
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Inherited human PGAM2 (PGAM-M) deficiency causes glycogen storage disease type X with exercise intolerance and cramps, underscoring its essential role in high-flux muscle glycolysis.
"Heart-focused work cites that **human PGAM deficiency** causes **glycogen storage disease type X**, characterized by **exercise intolerance and cramps**, consistent with an essential role for PGAM2 in high-flux muscle glycolysis"