PMID:10437801
| Citation |
Fraser, HI, Kvaratskhelia, M and White, MF (1999) The two analogous phosphoglycerate mutases of Escherichia coli. FEBS Lett. 455:344-8 |
|---|---|
| Abstract |
The glycolytic enzyme phosphoglycerate mutase exists in two evolutionarily unrelated forms. Vertebrates have only the 2,3-bisphosphoglycerate-dependent enzyme (dPGM), whilst higher plants have only the cofactor-independent enzyme (iPGM). Certain eubacteria possess genes encoding both enzymes, and their respective metabolic roles and activities are unclear. We have over-expressed, purified and characterised the two PGMs of Escherichia coli. Both are expressed at high levels, but dPGM has a 10-fold higher specific activity than iPGM. Differential inhibition by vanadate was observed. The presence of an integral manganese ion in iPGM was confirmed by EPR spectroscopy. |
| Links | |
| Keywords |
Animals; Base Sequence; DNA Primers/genetics; Electron Spin Resonance Spectroscopy; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Gene Expression; Genes, Bacterial; Isoenzymes/antagonists & inhibitors; Isoenzymes/genetics; Isoenzymes/metabolism; Kinetics; Manganese/chemistry; Molecular Sequence Data; Phosphoglycerate Mutase/antagonists & inhibitors; Phosphoglycerate Mutase/genetics; Phosphoglycerate Mutase/metabolism; Vanadates/pharmacology |
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