ArticleBiochemistry2016
Chemical Mechanism of the Branched-Chain Aminotransferase IlvE from Mycobacterium tuberculosis.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Role of Aspartate 86 in the Catalytic Mechanism ofBiochemistry · 2026Article
- Amino Acid Biosynthesis Inhibitors in Tuberculosis Drug Discovery.Pharmaceutics · 2024Review
- To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme fromMolecules (Basel, Switzerland) · 2023Article
- Research progress on branched-chain amino acid aminotransferases.Frontiers in genetics · 2023Review
- Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis.Nature communications · 2020Article
- Review
- Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms, and Drugability.Biochemistry · 2017Review
- Mechanism-Based Inhibition of the Mycobacterium tuberculosis Branched-Chain Aminotransferase by d- and l-Cycloserine.ACS chemical biology · 2017Article
- Acetolactate synthase regulatory subunits play divergent and overlapping roles in branched-chain amino acid synthesis and Arabidopsis development.BMC plant biology · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The biosynthetic pathway of the branched-chain amino acids is essential for Mycobacterium tuberculosis growth and survival. We report here the kinetic and chemical mechanism of the pyridoxal 5'-phosphate (PLP)-dependent branched-chain aminotransferase, IlvE, from M. tuberculosis (MtIlvE). This enzyme is responsible for the final step of the synthesis of the branched-chain amino acids isoleucine, leucine, and valine. As seen in other aminotransferases, MtIlvE displays a ping-pong kinetic mechanism. pK values were identified from the pH dependence on V as well as V/K, indicating that the phosphate ester of the PLP cofactor, and the α-amino group from l-glutamate and the active site Lys
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Registered trials
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