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Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate.
Additional recommended knowledge
PGM is a transferase enzyme, effectively transferring a phosphate group (HPO32-) from the C-3 carbon of 3-phosphoglycerate to the C-2 carbon forming 2-phosphoglycerate. It should be noted that the reaction involves two separate phosphoryl groups and the ending phosphate on the 2-carbon is not the same phosphate removed from the 3-carbon.
3PG + P-Enzyme → 2,3BPG + Enzyme → 2PG + P-Enzyme
3-phosphoglycerate intermediate 2-phosphoglycerate
Phosphoglycerate mutase exists primarily as a dimer of two either identical or closely related subunits of about 32kDa. The enzyme is found in organisms as simple as yeast through homo sapiens and its structure is highly conserved throughout. (Yeast PGM≈74% conserved vs mammal form).
Phosphoglycerate mutase has a small positive Gibbs free energy and this reaction proceeds easily in both directions. Since it is a reversible reaction, it is not the site of major regulation mechanisms or regulation schemes for the glycolytic pathway.
In humans, deficiency in phophoglycerate mutase function presents as a a metabolic myopathy and is one of the many forms of syndromes formerly referred to as muscular dystrophy. Dysfunction in the activity of phosphoglycerate mutase is an autosomal recessive genetic disorder with symtpoms ranging from mild to moderate, is not thought life-threatening and can be managed with changes in lifestyle.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Phosphoglycerate_mutase". A list of authors is available in Wikipedia.|