Psychiatry related information on PGM1

• These results suggest that phosphoglucomutase activity may be significant in patients with bipolar disorder treated with lithium and carbamazepine [1].

High impact information on PGM1

• Two of the suppressors, pgm1-1 and pgm1-2, are mutant alleles of PGM1 which encodes a glycolytic enzyme, phosphoglycerate mutase [2].
• The Saccharomyces cerevisiae GAL5 (PGM2) gene was isolated and shown to encode the major isozyme of phosphoglucomutase [3].
• Transcription of a yeast phosphoglucomutase isozyme gene is galactose inducible and glucose repressible [3].
• PGM is an enzyme that interconverts glucose-1 phosphate and glucose-6 phosphate and is regulated by Msn2p at the transcriptional level [4].
• Lithium acts as a competitive inhibitor of yeast phosphoglucomutase activity by competing with magnesium, a cofactor of the enzyme [5].

Biological context of PGM1

• The over-expression of PGM1 was not able to suppress any other RAS2(val19) phenotype or the galactose growth defect associated with a gal1Delta mutant [6].
• By subcloning of the yeast DNA insertions of the plasmids originally isolated the PGM1 coding region was located within a 1.3 kb SalI-HindIII fragment [7].
• The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae [8].
• Inhibition of phosphoglucomutase activity by lithium alters cellular calcium homeostasis and signaling in Saccharomyces cerevisiae [9].
• The enzyme phosphoglucomutase functions at a key point in carbohydrate metabolism [10].

Anatomical context of PGM1

• Erythrocyte phosphoglucomutase activity of bipolar I patients currently using lithium or carbamazepine [1].

Associations of PGM1 with chemical compounds

• Overall, these data suggest that the elevated levels of phosphoglucomutase activity allow for the more efficient utilization of the limiting levels of glucose-1-phosphate that are present in the RAS2(val19) mutant [6].
• Phosphoglucomutase is the acceptor for UDP-glucose: glycoprotein glucose-1-phosphotransferase and contains Glc in a phosphodiester linkage to O-linked Man. In this study, we have characterized the glycosylation of phosphoglucomutase by Saccharomyces cerevisiae in response to heat shock and growth in media containing carbon sources other than Glc [8].
• The glucosylation state of phosphoglucomutase was also compared in cells grown in media containing various carbon sources and was found to be lowest in cells utilizing Gal as the sole carbon source compared with Glc or lactate [8].
• Based on our findings, we concluded that phosphoglucomutase plays a key role in controlling the flux through the Leloir pathway, probably due to increased conversion of glucose-1-phosphate to glucose-6-phosphate [11].
• We found that Li+ inhibition of phosphoglucomutase causes a similar elevation of total cellular Ca2+ and an increase in 45Ca2+ uptake in a wild-type yeast strain grown in medium containing galactose, but not glucose, as sole carbon source [9].

Other interactions of PGM1

• This screen identified two genes, PGM1 and PCM1, that encode proteins with phosphoglucomutase activity [6].
• These observations suggest that Li+ inhibition of phosphoglucomutase results in an increased glucose-1-phosphate-to-glucose-6-phosphate ratio, which results in an accelerated rate of vacuolar Ca2+ uptake via the Ca2+-ATPase Pmc1p [9].
• A further reduction of flux towards UDP-Glc was achieved by deletion of the two phosphoglucomutase genes in the ugp1 conditional strain [12].
• Interestingly these molecular weights could correspond to the subunit of trehalose-6-phosphate synthase and to phosphoglucomutase II, respectively [13].
• Cibacron Blue chromatography was found useful at an early stage of purification for the removal of contaminating hexokinase, phosphoglucose isomerase and phosphoglucomutase [14].

References