Allosteric pyruvate kinase-based "logic gate" synergistically senses energy and sugar levels in Mycobacterium tuberculosis

• Main Authors: Zhong, W, Cui, L, Goh, B.C, Cai, Q, Ho, P, Chionh, Y.H, Yuan, M, Sahili, A.E, Fothergill-Gilmore, L.A, Walkinshaw, M.D, Lescar, J, Dedon, P.C
• Other Authors: DUKE-NUS MEDICAL SCHOOL
• Format: Article
• Published: Nature Publishing Group 2020
• Subjects: adenosine phosphate; glucose 6 phosphate; pyruvate kinase; glucose; energy; enzyme activity; metabolism; metabolite; network analysis; nutrient; sugar; tuberculosis; allosteric site; allosterism; amino acid sequence; Article; carboxy terminal sequence; comparative study; conformational transition; controlled study; energy metabolism; enzyme activation; enzyme kinetics; enzyme stability; enzyme structure; gene expression system; glucose metabolism; metabolic regulation; molecular dynamics; Mycobacterium bovis BCG; nonhuman; protein protein interaction; chemistry; enzyme assay; kinetics; metabolome; metabolomics; molecular docking; Mycobacterium bovis; Mycobacterium tuberculosis; protein domain; X ray crystallography; Bacteria (microorganisms); Adenosine Monophosphate; Allosteric Regulation; Crystallography, X-Ray; Enzyme Assays; Glucose; Glucose-6-Phosphate; Kinetics; Metabolome; Metabolomics; Molecular Docking Simulation; Protein Domains; Pyruvate Kinase
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/178553
• Institution: National University of Singapore

10.1038/s41467-017-02086-y