Pyruvate‐formate‐lyase‐deactivase and acetyl‐CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE

@article{Kessler1991PyruvateformatelyasedeactivaseAA,
  title={Pyruvate‐formate‐lyase‐deactivase and acetyl‐CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE},
  author={Dorothea Kessler and Iris Leibrecht and J. Knappe},
  journal={FEBS Letters},
  year={1991},
  volume={281}
}
A 4.8 kb DNA‐fragment was cloned and sequenced encompassing the structural gene of PFL‐deactivase (2.7 kb) and 2 kb of the 5 flanking region that contains the elements for anaerobic induction. A mutant lacking deactivase was shown to require exogenous electron acceptors for anaecrobic growth with glucose. This revealed the identity of PFL‐deactivase with the alcohol and acetaldehyde dehydrogenases of E. coli. The multienzyme represents a homopolymeric protein (∼ 40 × 96 kDa) requiring Fe2+ for… Expand
Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules.
TLDR
It is demonstrated that E. coli AdhE is not a PFL deactivating enzyme, and the potential for deactivation of active PFL by small-molecule thiols is examined, with the former providing quite rapid deactivation. Expand
Pyruvate formate-lyase (PFL)
1. Summary Pyruvate formate-lyase (PFL) is an important enzyme in the metabolic pathway of lactic acid bacteria (LAB) and is held responsible for the regulation of the shift between homolactic acidExpand
Molecular properties of pyruvate formate-lyase activating enzyme.
TLDR
Kinetic studies showed that the rate of radical formation was independent of ionic strength and the Km's for SAM and inactive PFL were determined to be 2.8 and 1.2 microM, respectively, indicating that the binding site for SAM resides on AE. Expand
Molecular characteristics and transcription of the gene encoding a multifunctional alcohol dehydrogenase in relation to the deactivation of pyruvate formate-lyase in the ruminal bacterium Streptococcus bovis
TLDR
It is conceivable that ADHE is not significantly involved in the reversible inactivation of active PFL under anoxic conditions, and partition of the flow from pyruvate appears to be mainly regulated by the activities of lactate dehydrogenase and PFL. Expand
Evolution of the adhE gene product of Escherichia coli from a functional reductase to a dehydrogenase. Genetic and biochemical studies of the mutant proteins.
TLDR
It appears that when AdhE catalyzes the two sequential reactions in the counter-physiological direction, acetaldehyde dehydrogenation is the rate-limiting step. Expand
Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri
TLDR
A region of genomic DNA from Clostridium kluyveri was cloned in Escherichia coli by a screening strategy which was based on heterologous expression of the clostridial 4-hydroxybutyrate dehydrogenase gene, and similarities to the adhE (aad) gene products from E. coli were revealed. Expand
Regulation of adhE (Encoding Ethanol Oxidoreductase) by the Fis Protein in Escherichia coli
TLDR
It is shown that the expression of adhE also depends on the Fis (factor for inversion stimulation) protein, and a strain bearing a fis::kan null allele failed to grow anaerobically on glucose solely because of inadequateadhE transcription. Expand
Biochemical and Physiological Characterization of the Pyruvate Formate-Lyase Pfl1 of Chlamydomonas reinhardtii, a Typically Bacterial Enzyme in a Eukaryotic Alga
TLDR
The formate-producing activity of the putative Pfl1 enzyme is proved by heterologous expression of the C. reinhardtii PFL1 cDNA in Escherichia coli and subsequent in vitro activity tests of the purified protein. Expand
A bacterial hydrogen‐dependent CO2 reductase forms filamentous structures
TLDR
The further characterization of the quaternary structure of this enzymes complex is described and the unexpected behavior of this enzyme in polymerizing into filamentous structures is described. Expand
Cloning, Expression, Primary Structure, and Insertion Mutagenesis of the Pyruvate Formate-Lyase Enzyme of Aeromonas Hydrophila.
TLDR
The pyruvate formate-lyase gene (pfl) of the facultative anaerobe Aeromonas hydrophila was cloned and sequenced, and the Pfl was characterized based on the deduced amino acid sequence and evaluated in vivo following insertion mutagenesis. Expand
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