ArticleNature chemical biology2013
Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 58 citations in OpenAlex.
- The Evolution of the First Code.Genes · 2026Review
- Evolution of lysine and arginine biosynthesis revealed by substrate specificity of lysine biosynthetic enzymes in Thermus thermophilus.The FEBS journal · 2026Article
- Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function.FEBS letters · 2025Article
- Dissecting the Arginine and Lysine Biosynthetic Pathways and Their Relationship in Haloarchaeon Natrinema gari J7-2 via Endogenous CRISPR-Cas System-Based Genome Editing.Microbiology spectrum · 2023Article
- AlphaFold Accurately Predicts the Structure of Ribosomally Synthesized and Post-Translationally Modified Peptide Biosynthetic Enzymes.Biomolecules · 2023Article
- Prebiotic Synthesis of Aspartate Using Life's Metabolism as a Guide.Life (Basel, Switzerland) · 2023Article
- Transcriptome profiling of Nudix hydrolase gene deletions in the thermoacidophilic archaeonFrontiers in microbiology · 2023Article
- Biosynthesis of 3-thia-α-amino acids on a carrier peptide.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Encapsulins.Annual review of biochemistry · 2022Review
- Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB.Nature chemical biology · 2021Article
- Large-scale computational discovery and analysis of virus-derived microbial nanocompartments.Nature communications · 2021Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- Structural Basis for a Dual Function ATP Grasp Ligase That Installs Single and Bicyclic ω-Ester Macrocycles in a New Multicore RiPP Natural Product.Journal of the American Chemical Society · 2021Article
- Machine Learning Uncovers a Data-Driven Transcriptional Regulatory Network for the Crenarchaeal ThermoacidophileFrontiers in microbiology · 2021Article
- Use of a scaffold peptide in the biosynthesis of amino acid-derived natural products.Science (New York, N.Y.) · 2019Article
- Structural polymorphism of the Escherichia coli poly-α-L-glutamate synthetase RimK.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Genome-scale metabolic model analysis indicates low energy production efficiency in marine ammonia-oxidizing archaea.AMB Express · 2018Article
- Early Response ofFrontiers in microbiology · 2018Article
- Large-scale computational drug repositioning to find treatments for rare diseases.NPJ systems biology and applications · 2018Article
- Recent Advances in Our Understanding of the Biosynthesis of Sulfur Modifications in tRNAs.Frontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
17 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LysW has been identified as a carrier protein in the lysine biosynthetic pathway that is active through the conversion of α-aminoadipate (AAA) to lysine. In this study, we found that the hyperthermophilic archaeon, Sulfolobus acidocaldarius, not only biosynthesizes lysine through LysW-mediated protection of AAA but also uses LysW to protect the amino group of glutamate in arginine biosynthesis. In this archaeon, after LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. The crystal structure of ArgX, the enzyme responsible for modification and protection of the amino moiety of glutamate with LysW, was determined in complex with LysW. Structural comparison and enzymatic characterization using Sulfolobus LysX, Sulfolobus ArgX and Thermus LysX identify the amino acid motif responsible for substrate discrimination between AAA and glutamate. Phylogenetic analysis reveals that gene duplication events at different stages of evolution led to ArgX and LysX.
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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.