An In Vivo Metabolic Approach for Deciphering the Product Specificity of 
Glycerate Kinase Proves that Both E. coli's Glycerate Kinases Generate 
2-Phosphoglycerate

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

doi:10.1371/journal.pone.0122957

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

An In Vivo Metabolic Approach for Deciphering the Product Specificity of Glycerate Kinase Proves that Both E. coli's Glycerate Kinases Generate 2-Phosphoglycerate

MPS-Authors

/persons/resource/persons132110

Bar-Even, A.
Systems and Synthetic Metabolism, Max Planck Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Zelcbuch, L., Razo-Mejia, M., Herz, E., Yahav, S., Antonovsky, N., Kroytoro, H., et al. (2015). An In Vivo Metabolic Approach for Deciphering the Product Specificity of Glycerate Kinase Proves that Both E. coli's Glycerate Kinases Generate 2-Phosphoglycerate. PLoS One, 10(3): e0122957. doi:10.1371/journal.pone.0122957.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0027-9DA5-6

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.