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The two analogous phosphoglycerate mutases of Escherichia coli
Author(s) -
Fraser Heather I,
Kvaratskhelia Mamuka,
White Malcolm F
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00910-2
Subject(s) - phosphoglycerate mutase , phosphoglycerate kinase , escherichia coli , enzyme , vanadate , biochemistry , biology , mutase , cofactor , gene , chemistry , glycolysis
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.