Journal
BIOCHEMISTRY
Volume 55, Issue 17, Pages 2423-2426Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00184
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Funding
- Max Planck Society
- European Commission Horizon 2020 FETOpen grant [686330]
- European Research Council [260392]
- Helmsley Charitable Foundation
- Israel Ministry of Science
- European Research Council (ERC) [260392] Funding Source: European Research Council (ERC)
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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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