ReviewFrontiers in molecular biosciences2022
Structural Basis for Allostery in PLP-dependent Enzymes.
Review in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- Pyridoxal-phosphate-dependent biosynthesis of aminovaleramide by AvaS in tRNA.Nature chemical biology · 2026Article
- Transaminases engineering and their cascade systems for natural product synthesis.Applied biochemistry and biotechnology · 2026Review
- Molecular Basis of GABA Aminotransferase Inhibition in Epilepsy: Structure, Mechanisms, and Drug Development.Current issues in molecular biology · 2025Review
- Vitamin biosynthesis in the gut: interplay between mammalian host and its resident microbiota.Microbiology and molecular biology reviews : MMBR · 2025Review
- Genomic Insights into Vector-Pathogen Adaptation inPathogens (Basel, Switzerland) · 2025Article
- Diversity and distribution of amino acid decarboxylase enzymes in the human gut bacteria-a bioinformatics investigation.Frontiers in microbiology · 2025Article
- Structure simulation-based comparison of active site variations in fungal ornithine decarboxylases.Communicative & integrative biology · 2025Article
- From Structure to Function: Analysis of the First Monomeric Pyridoxal-5'-Phosphate-Dependent Transaminase from the BacteriumBiomolecules · 2024Article
- A computational strategy to improve the activity of tyrosine phenol-lyase for the synthesis of L-DOPA.Scientific reports · 2024Article
- Efficient biosynthesis of D/L-alanine in the recombinantFrontiers in bioengineering and biotechnology · 2024Article
- Kinetic Characterization and Catalytic Mechanism ofInternational journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Pyridoxal 5'-phosphate (PLP)-dependent enzymes are found ubiquitously in nature and are involved in a variety of biological pathways, from natural product synthesis to amino acid and glucose metabolism. The first structure of a PLP-dependent enzyme was reported over 40 years ago, and since that time, there is a steady wealth of structural and functional information revealed for a wide array of these enzymes. A functional mechanism that is gaining more appreciation due to its relevance in drug design is that of protein allostery, where binding of a protein or ligand at a distal site influences the structure, organization, and function at the active site. Here, we present a review of current structure-based mechanisms of allostery for select members of each PLP-dependent enzyme family. Knowledge of these mechanisms may have a larger potential for identifying key similarities and differences among enzyme families that can eventually be exploited for therapeutic development.
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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.