Phosphoglycerate Mutase Is a Highly Efficient Enzyme without Flux Control in Lactococcus lactis

Publication: Research - peer-reviewJournal article – Annual report year: 2010

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The glycolytic enzyme phosphoglycerate mutase (PGM), which catalyzes the conversion of 3-phosphoglycerate to 2-phosphoglycerate, was examined in Lactococcus lactis with respect to its function, kinetics and glycolytic flux control. A library of strains with PGM activities ranging between 15-465% of the wild-type level was constructed by replacing the native promoter of pgm with synthetic promoters of varying strengths. The specific growth rate and glucose flux were found to be maximal at the wild-type level at which PGM had no flux control. Low flux control of PGM was found on mixed acid fluxes at highly reduced PGM activities. At the wild-type level PGM operated very far from V-max. Consequently, in a strain with only 15% PGM activity, the catalytic rate of PGM was almost six times higher than in the wildtype. K-m of PGM for 3-phosphoglycerate was 1.0 m M and k(cat) was 3,200 s(-1). The L. lactis PGM was dependent on 2,3-bisphosphoglyceric acid for activity, which showed that the enzyme is of the dPGM type in accordance with its predicted homology to dPGM enzymes from other organisms. In conclusion, PGM from L. lactis is a highly efficient catalyst, which partially explains why this enzyme has limited control in wild-type L. lactis.
Original languageEnglish
JournalJournal of Molecular Microbiology and Biotechnology
Publication date2010
Volume18
Issue3
Pages174-180
ISSN1464-1801
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 6

Keywords

  • Metabolic control analysis, Lactic acid bacteria, Phosphoglycerate mutase, Systems biology, Glycolysis, Metabolism
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