Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase (Q27619164)

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M C Merckel

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D L Ollis

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K K Wong

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J W Kozarich

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A Goldman

Post-translational activation introduces a free radical into pyruvate formate-lyase

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publication date

15 July 1999

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published in

Structure

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volume

7

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page(s)

733-44

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issue

7

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cites work

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The free radical in pyruvate formate-lyase is located on glycine-734

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Glycyl free radical in pyruvate formate-lyase: synthesis, structure characteristics, and involvement in catalysis.

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Inactivation of Escherichia coli pyruvate formate-lyase by hypophosphite: evidence for a rate-limiting phosphorus-hydrogen bond cleavage

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Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate

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Dioxygen inactivation of pyruvate formate-lyase: EPR evidence for the formation of protein-based sulfinyl and peroxyl radicals

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Pyruvate formate-lyase mechanism involving the protein-based glycyl radical

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

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Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism.

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Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase

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Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli

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A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene

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A Glycyl Radical Site in the Crystal Structure of a Class III Ribonucleotide Reductase

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Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding

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Structure of ribonucleotide reductase protein R1

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Protein structure comparison by alignment of distance matrices

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Purification and crystallization of a proteolytic fragment of Escherichia coli pyruvate formate-lyase

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The B12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: an evolutionary solution to the ribonucleotide reductase conundrum

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Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalyzed by cysteine 419

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Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes?

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Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme

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Identifiers

DOI

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Fatcat ID

release_6z4togz62zb33ikls26mqwnlzu

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Fatcat

https://api.fatcat.wiki/v0/release/6z4togz62zb33ikls26mqwnlzu

24 November 2022