Determination of Pre-Steady-State Rate Constants on the Escherichia coli Pyruvate Dehydrogenase Complex Reveals That Loop Movement Controls the Rate-Limiting Step
Author:
Affiliation:
1. Department of Chemistry, Rutgers the State University, Newark, New Jersey 07102, United States
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja3062375
Reference55 articles.
1. α-Keto Acid Dehydrogenation Complexes
2. The Pyruvate Dehydrogenase Complex of Escherichia coli K12. Nucleotide Sequence Encoding the Pyruvate Dehydrogenase Component
3. The Pyruvate Dehydrogenase Complex of Escherichia coli K12. Nucleotide Sequence Encoding the Dihydrolipoamide Acetyltransferase Component
4. Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12
5. A Thiamin-bound, Pre-decarboxylation Reaction Intermediate Analogue in the Pyruvate Dehydrogenase E1 Subunit Induces Large Scale Disorder-to-Order Transformations in the Enzyme and Reveals Novel Structural Features in the Covalently Bound Adduct
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