ArticlePLoS computational biology2018
Structural and dynamic basis of substrate permissiveness in hydroxycinnamoyltransferase (HCT).
Article in PLoS computational biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 45 citations in OpenAlex.
- Advances in the Function Roles of Hydroxycinnamoyl-CoA Shikimate/Quinate Hydroxycinnamoyl Transferases: A Key Enzyme Linking Phenylpropanoid Metabolism to Plant Terrestrial Adaptation.Plants (Basel, Switzerland) · 2026Review
- Metabolic engineeringSynthetic and systems biotechnology · 2025Article
- Mechanistic basis for the emergence of EPS1 as a catalyst in salicylic acid biosynthesis of Brassicaceae.Nature communications · 2024Article
- Uncovering the Role of Hydroxycinnamoyl Transferase in Boosting Chlorogenic Acid Accumulation inInternational journal of molecular sciences · 2024Article
- Analysing a Group of Homologous BAHD Enzymes Provides Insights into the Evolutionary Transition of Rosmarinic Acid Synthases from Hydroxycinnamoyl-CoA:Shikimate/Quinate Hydroxycinnamoyl Transferases.Plants (Basel, Switzerland) · 2024Article
- Family characteristics, phylogenetic reconstruction, and potential applications of the plant BAHD acyltransferase family.Frontiers in plant science · 2023Review
- Article
- Crowding within synaptic junctions influences the degradation of nucleotides by CD39 and CD73 ectonucleotidases.Biophysical journal · 2022Article
- Characterization of evolutionarily distinct rice BAHD-Acyltransferases provides insight into their plausible role in rice susceptibility to Rhizoctonia solani.The plant genome · 2021Article
- Function of the HYDROXYCINNAMOYL-CoA:SHIKIMATE HYDROXYCINNAMOYL TRANSFERASE is evolutionarily conserved in embryophytes.The Plant cell · 2021Article
- Cell-Free Expression of a Plant Membrane Protein BrPT2 From Boesenbergia Rotunda.Molecular biotechnology · 2021Article
- Article
- Genome-wide analysis of the lignin toolbox forPeerJ · 2021Article
- Crystal structure of barley agmatine coumaroyltransferase, an N-acyltransferase from the BAHD superfamily.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Parameterization of a drug molecule with a halogen σ-hole particle using ffTK: Implementation, testing, and comparison.The Journal of chemical physics · 2020Article
- Structural and Biochemical Insights Into Two BAHD Acyltransferases (Frontiers in plant science · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Substrate permissiveness has long been regarded as the raw materials for the evolution of new enzymatic functions. In land plants, hydroxycinnamoyltransferase (HCT) is an essential enzyme of the phenylpropanoid metabolism. Although essential enzymes are normally associated with high substrate specificity, HCT can utilize a variety of non-native substrates. To examine the structural and dynamic basis of substrate permissiveness in this enzyme, we report the crystal structure of HCT from Selaginella moellendorffii and molecular dynamics (MD) simulations performed on five orthologous HCTs from several major lineages of land plants. Through altogether 17-μs MD simulations, we demonstrate the prevalent swing motion of an arginine handle on a submicrosecond timescale across all five HCTs, which plays a key role in native substrate recognition by these intrinsically promiscuous enzymes. Our simulations further reveal how a non-native substrate of HCT engages a binding site different from that of the native substrate and diffuses to reach the catalytic center and its co-substrate. By numerically solving the Smoluchowski equation, we show that the presence of such an alternative binding site, even when it is distant from the catalytic center, always increases the reaction rate of a given substrate. However, this increase is only significant for enzyme-substrate reactions heavily influenced by diffusion. In these cases, binding non-native substrates 'off-center' provides an effective rationale to develop substrate permissiveness while maintaining the native functions of promiscuous enzymes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.