High impact information on Pgam1

• An unbiased screen for genes that can immortalize mouse embryonic fibroblasts identified the glycolytic enzyme phosphoglycerate mutase (PGM) [1].
• Glucosephosphate isomerase, another glycolytic enzyme, displays similar activity and, conversely, depletion of PGM or glucosephosphate isomerase with short interfering RNA triggers premature senescence [1].
• Old mice on CR showed significant decreases in the activities of all the enzymes studied, except for aldolase, triosephosphate isomerase and phosphoglycerate mutase, which were unchanged [2].
• A precise localization of a mouse gene encoding increased phosphoglycerate mutase activity (Pgam1e1) on chromosome 19 [3].
• Amino acid residues which are most likely critical for either 2,3-bisphosphoglycerate mutase or phosphoglycerate mutase function are pointed out [4].

Biological context of Pgam1

• The activities of glutamate oxaloacetate transaminase-1 and phosphoglycerate mutase-1 are increased by 50%, compatible with a gene dosage effect of these two enzymes [5].

Anatomical context of Pgam1

• Extracts of embryonic mouse tissues (skeletal, cardiac and smooth muscle, and brain) were analysed by Cellogel electrophoresis for their isoenzymic distributions of three enzymes, creatine phosphokinase, aldolase and phosphoglycerate mutase [6].

Associations of Pgam1 with chemical compounds

• Amino acid alignment with the other related enzymes, the phosphoglycerate mutases, in combination with crystallographic data from yeast phosphoglycerate mutase, gives some insight into the structure/function correlation for this protein family [4].
• However, phosphoglycerate mutase contained small amounts of covalently bound 32P that was exchangeable with 3-phosphoglycerate and therefore, most likely was incorporated during the catalytic reaction cycle [7].
• Isoenzyme transitions of creatine phosphokinase, aldolase and phosphoglycerate mutase in differentiating mouse cells [6].

Other interactions of Pgam1

• Crystallization and initial crystal characterization of the C-terminal phosphoglycerate mutase homology domain of Sts-1 [8].

References