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  • Title: Pyruvate Formate-Lyase Enables Efficient Growth of Escherichia coli on Acetate and Formate.
    Author: Zelcbuch L, Lindner SN, Zegman Y, Vainberg Slutskin I, Antonovsky N, Gleizer S, Milo R, Bar-Even A.
    Journal: Biochemistry; 2016 May 03; 55(17):2423-6. PubMed ID: 27093333.
    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.
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