Pyruvate formate-lyase enables efficient growth of Escherichia coli on acetate and formate

Lior Zelcbuch, Steffen N. Lindner, Yonatan Zegman, Ilya Vainberg Slutskin, Niv Antonovsky, Shmuel Gleizer, Ron Milo, Arren Bar-Even

Research output: Contribution to journalArticlepeer-review

Abstract

Pyruvate formate-lyase (PFL) is a ubiquitous enzyme that supports increased ATP yield during sugar fermentation. While the PFL reaction is known to be reversible in vitro, the ability of PFL to support microbial growth by condensing acetyl-CoA and formate in vivo has never been directly tested. Here, we employ Escherichia coli mutant strains that cannot assimilate acetate via the glyoxylate shunt and use carbon labeling experiments to unequivocally demonstrate PFL-dependent co-assimilation of acetate and formate. Moreover, PFL-dependent growth is faster than growth on acetate using the glyoxylate shunt. Hence, growth via the reverse activity of PFL could have substantial ecological and biotechnological significance.

Original languageEnglish
Pages (from-to)2423-2426
Number of pages4
JournalBiochemistry
Volume55
Issue number17
Early online date21 Apr 2016
DOIs
StatePublished - 3 May 2016

All Science Journal Classification (ASJC) codes

  • Biochemistry

Fingerprint

Dive into the research topics of 'Pyruvate formate-lyase enables efficient growth of Escherichia coli on acetate and formate'. Together they form a unique fingerprint.

Cite this