Novel keto acid formate‐lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L‐threonine to propionate

@article{Hesslinger1998NovelKA,
  title={Novel keto acid formate‐lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L‐threonine to propionate},
  author={C. Hesslinger and S. Fairhurst and G. Sawers},
  journal={Molecular Microbiology},
  year={1998},
  volume={27}
}
An immunological analysis of an Escherichia coli strain unable to synthesize the main pyruvate formate‐lyase enzyme Pfl revealed the existence of a weak, cross‐reacting 85 kDa polypeptide that exhibited the characteristic oxygen‐dependent fragmentation typical of a glycyl radical enzyme. Polypeptide fragmentation of this cross‐reacting species was shown to be dependent on Pfl activase. Cloning and sequence analysis of the gene encoding this protein revealed that it coded for a new enzyme… Expand
The Glycyl Radical Enzyme TdcE Can Replace Pyruvate Formate-Lyase in Glucose Fermentation
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It is shown that TdcE is directly responsible for the restoration of fermentative growth to pfl mutants, one of the products encoded by the tdc operon, TDCE, that can accept pyruvate as an enzyme substrate. Expand
The glycyl-radical enzyme 2-ketobutyrate formate-lyase, TdcE, interacts specifically with the formate-translocating FNT-channel protein FocA
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1 Coordinating FocA and Pyruvate Formate-Lyase Synthesis in Escherichia coli : 1 Preferential Translocation of Formate Over Other Mixed-Acid Fermentation 2 Products 3 4
26 Enterobacteria like Escherichia coli generate formate, lactate, acetate and succinate as major 27 acidic fermentation products. Accumulation of these products in the cytoplasm would lead to 28Expand
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Structure and function of enzymes involved in the anaerobic degradation of L-threonine to propionate
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Activation of glyoxylate pathway without the activation of its related gene in succinate-producing engineered Escherichia coli.
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