ArticleChembiochem : a European journal of chemical biology2019
Generation of a Stand-Alone Tryptophan Synthase α-Subunit by Mimicking an Evolutionary Blueprint.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Inactive but Essential: The Role of the Inactive State of E49 in the Mechanism of the Alpha Subunit of Tryptophan Synthase and Its Stand-Alone BlueprintACS catalysis · 2026Article
- Independent evolution of plant natural products: Formation of benzoxazinoids in Consolida orientalis (Ranunculaceae).The Journal of biological chemistry · 2025Article
- Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha Subunit.ACS catalysis · 2024Article
- Expanding the viewpoint: Leveraging sequence information in enzymology.Current opinion in chemical biology · 2023Review
- Fermentative Indole Production via Bacterial Tryptophan Synthase Alpha Subunit and Plant Indole-3-Glycerol Phosphate Lyase Enzymes.Journal of agricultural and food chemistry · 2022Article
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- Rapid online buffer exchange for screening of proteins, protein complexes and cell lysates by native mass spectrometry.Nature protocols · 2020Article
- Quaternary Structure of the Tryptophan Synthase α-Subunit Homolog BX1 fromJournal of the American Society for Mass Spectrometry · 2020Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The αββα tryptophan synthase (TS), which is part of primary metabolism, is a paradigm for allosteric communication in multienzyme complexes. In particular, the intrinsically low catalytic activity of the α-subunit TrpA is stimulated several hundredfold through the interaction with the β-subunit TrpB1. The BX1 protein from Zea mays (zmBX1), which is part of secondary metabolism, catalyzes the same reaction as that of its homologue TrpA, but with high activity in the absence of an interaction partner. The intrinsic activity of TrpA can be significantly increased through the exchange of several active-site loop residues, which mimic the corresponding loop in zmBX1. The subsequent identification of activating amino acids in the generated "stand-alone" TrpA contributes to an understanding of allostery in TS. Moreover, findings suggest an evolutionary trajectory that describes the transition from a primary metabolic enzyme regulated by an interaction partner to a self-reliant, stand-alone, secondary metabolic enzyme.
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