phosphoglyceromutase

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phos·pho·glyc·er·o·mu·tase

(fos'fō-glis'ĕr-ō-myū'tās),
An isomerizing enzyme catalyzing the reversible interconversion of 2-phosphoglycerate and 3-phosphoglycerate with 2,3-bisphosphoglycerate present as a cofactor; a deficiency of this enzyme, which plays a role in glycolysis, is an inherited disorder that results in an intolerance for strenuous exercise.

phosphoglyceromutase

(fos″fō″glis″ĕ-rō-mū′tās″) [ phospho- + glycero- + mutase],

PGM

A red blood cell enzyme that participates in the metabolism of glucose.
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References in periodicals archive ?
Downstream of the necrosome are two splice variants of phosphoglycerate mutase family member 5 (PGAM5), PGAM5S and PGAM5L.
gpmA and eno encode phosphoglycerate mutase and enolase, respectively, which have been known to participate in substrate level phosphorylation as glycolytic enzymes in carbon metabolism.
Nevertheless, PEP may promote the production of pyruvate independent of PKM2 activity through serving as a phosphodonor for phosphoglycerate mutase 1 (PGAM1) [66].
These include phosphoglycerate mutase 1 (PGAM1), triose phosphate isomerase (TPIS), and alpha enolase (ENOA).
The glycolysis genes include phosphoglycerate mutase 1 (5223), glyceraldehyde-3-phosphate dehydrogenase (2597), and glucose-6-phosphatase (57818).
2011, details unpublished), phosphoglycerate kinase (PfPGK) [24], and phosphoglycerate mutase (PfPGM) [25] have been solved.
The majority of these expressed proteins were involved in glycolysis (enolase, fructose-bisphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, L-lactate dehydrogenase, 6-phosphofructokinase, glucose-6-phosphate isomerase, phosphoglycerate kinase, phosphopyruvate hydratase, pyruvate kinase, triosephosphate isomerase, and 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase) and the remaining proteins were involved in fer-mentation (alcohol-acetaldehyde dehydrogenase, formate ace-tyltransferase, and pyruvate-formate lyase), the pentose phosphate pathway (6-phosphogluconate dehydrogenase [decarboxylating]), pyruvate decarboxylation (pyruvate dehydrogenase complex E2 component), and the urea cycle (ornithine carbamoyltransferase).
Molecular modeling, dynamics, and an insight into the structural inhibition of cofactor independent phosphoglycerate mutase isoform-1 from Wuchereria bancrofti using cheminformatics and mutational studies.
These genes include both the myosin heavy and light chain, and the phosphoglycerate mutase 2 (pgam2) gene.
(36) showed that biofilms of Staphylococcus aureus were upregulated for genes encoding enzymes involved in glycolysis or fermentation (phosphoglycerate mutase, triosephosphate isomerase, and alcohol dehydrogenase) and surmised that the up-regulation of these genes could be due to oxygen limitation in the developed biofilm, favoring fermentation.
Seven presumptive loci were reliably resolved in the snails: Pep-D (peptidase using Phe-Pro, 3.4.11), Idh-1 and Idh-2 (two isozymes of isocitrate dehydrogenase, 1.1.1.42), Pgm (phosphoglycerate mutase, 2.5.7.3), 6pgd (6-phosphogluconate dehydrogenase, 1.1.1.44), Mpi (man-nose-phosphate isomerase, 5.3.1.8), and Aat (aspartate aminotransferase, 2.6.11).

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