An in vivo metabolic approach for deciphering the product specificity of glycerate kinase proves that both E. coli's glycerate kinases generate 2-phosphoglycerate

Lior Zelcbuch, Manuel Razo-Mejia, Elad Herz, Sagit Yahav, Niv Antonovsky, Hagar Kroytoro, Ron Milo, Arren Bar-Even

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Apart from addressing humanity's growing demand for fuels, pharmaceuticals, plastics and other value added chemicals, metabolic engineering of microbes can serve as a powerful tool to address questions concerning the characteristics of cellular metabolism. Along these lines, we developed an in vivo metabolic strategy that conclusively identifies the product specificity of glycerate kinase. By deleting E. coli's phosphoglycerate mutases, we divide its central metabolism into an 'upper' and 'lower' metabolism, each requiring its own carbon source for the bacterium to grow. Glycerate can serve to replace the upper or lower carbon source depending on the product of glycerate kinase. Using this strategy we show that while glycerate kinase from Arabidopsis thaliana produces 3-phosphoglycerate, both E. coli' s enzymes generate 2-phosphoglycerate. This strategy represents a general approach to decipher enzyme specificity under physiological conditions.

Original languageEnglish
Article numbere0122957
JournalPLoS ONE
Volume10
Issue number3
DOIs
StatePublished - 30 Mar 2015
Externally publishedYes

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