In vitro reconstitution and characterization of pyruvate dehydrogenase and 2‐oxoglutarate dehydrogenase hybrid complex from Corynebacterium glutamicum
Author:
Affiliation:
1. Biotechnology Research Center The University of Tokyo Bunkyo‐ku Japan
2. Collaborative Research Institute for Innovative Microbiology The University of Tokyo Bunkyo‐ku Japan
3. RIKEN Center for Sustainable Resource Science Wako Japan
Funder
Japan Society for the Promotion of Science
Noda Institute for Scientific Research
Publisher
Wiley
Subject
Microbiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/mbo3.1113
Reference39 articles.
1. Novel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase‐dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complex;Arjunan P.;Journal of Biological Chemistry,2020
2. Dynamic and Structural Characterization of a Bacterial FHA Protein Reveals a New Autoinhibition Mechanism
3. Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli;Bennett B. D.;Nature Methods,2009
4. Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches
5. Molecular weight and symmetry of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
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3. Cellular localization of the hybrid pyruvate/2-oxoglutarate dehydrogenase complex in the actinobacteriumCorynebacterium glutamicum;Microbiology Spectrum;2023-10-17
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