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. (C) 1999 Federation of European Biochemical Societies.
| Original language | English |
|---|---|
| Pages (from-to) | 344-348 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 455 |
| Issue number | 3 |
| Publication status | Published - 23 Jul 1999 |
Keywords
- glycolysis
- phosphoglycerate mutase
- vanadate inhibition
- cofactor requirement
- Escherichia coli
- EXPRESSION
- FAMILY
- SYSTEM