The two analogous phosphoglycerate mutases of Escherichia coli.
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.
Fraser
H I
HI
Department of Biochemistry, University of Dundee, UK.
Kvaratskhelia
M
M
White
M F
MF
D000818:Animals; D001483:Base Sequence; D017931:DNA Primers / Q000235:genetics; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics* / Q000254:growth & development; D015870:Gene Expression; D005798:Genes, Bacterial; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000235:genetics* / Q000378:metabolism*; D007700:Kinetics; D008345:Manganese / Q000737:chemistry; D008969:Molecular Sequence Data; D010736:Phosphoglycerate Mutase / Q000037:antagonists & inhibitors / Q000235:genetics* / Q000378:metabolism*; D014638:Vanadates / Q000494:pharmacology
D017931:DNA Primers; D007527:Isoenzymes; D014638:Vanadates; D008345:Manganese; D010736:Phosphoglycerate Mutase