The Autonomous Glycyl Radical Protein GrcA Restores Activity to Inactive Full-Length Pyruvate Formate-Lyase In Vivo
Author:
Affiliation:
1. Institute for Biology/Microbiology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany
Abstract
Funder
Martin Luther University Halle-Wittenberg
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/jb.00070-22
Reference55 articles.
1. Post-translational activation introduces a free radical into pyruvate formate-lyase.
2. The free radical in pyruvate formate-lyase is located on glycine-734.
3. The Free Radical of the Anaerobic Ribonucleotide Reductase from Escherichia coli Is at Glycine 681
4. Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate
5. Biochemical and genetic characterization of benzylsuccinate synthase fromThauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism
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