ReviewTrends in biochemical sciences2018
Unraveling the Structure and Mechanism of the MST(ery) Enzymes.
Review in Trends in biochemical sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- (Reverse) Evolution of a Promiscuous Isochorismate Pyruvate Lyase into an Efficient Chorismate Mutase.Biochemistry · 2025Article
- Activity Regulation of a Glutamine Amidotransferase Bienzyme Complex by Substrate-Induced Subunit Interface Expansion.ACS catalysis · 2025Article
- Arabidopsis ICS1 produces salicylic acid precursor isochorismate through a gated channel mechanism.Plant physiology · 2024Article
- Structural Study of a New MbtI-Inhibitor Complex: Towards an Optimized Model for Structure-Based Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Diversity and functional traits of indigenous soil microbial flora associated with salinity and heavy metal concentrations in agricultural fields within the Indus Basin region, Pakistan.Frontiers in microbiology · 2022Article
- Salicylic Acid Biosynthesis and Metabolism: A Divergent Pathway for Plants and Bacteria.Biomolecules · 2021Review
- Plants fight fungi using kiwellin proteins.Nature · 2019Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The menaquinone, siderophore, and tryptophan (MST) enzymes transform chorismate to generate precursor molecules for the biosynthetic pathways defined in their name. Kinetic data, both steady-state and transient-state, and X-ray crystal structures indicate that these enzymes are highly conserved both in mechanism and in structure. Because these enzymes are found in pathogens but not in humans, there is considerable interest in these enzymes as drug design targets. While great progress has been made in defining enzyme structure and mechanism, inhibitor design has lagged behind. This review provides a detailed description of the evidence that begins to unravel the mystery of how the MST enzymes work, and how that information has been used in inhibitor design.
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Registered trials
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