ArticleThe Journal of biological chemistry2016
Lysine Biosynthesis of Thermococcus kodakarensis with the Capacity to Function as an Ornithine Biosynthetic System.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 25 citations in OpenAlex.
- Evolution of lysine and arginine biosynthesis revealed by substrate specificity of lysine biosynthetic enzymes in Thermus thermophilus.The FEBS journal · 2026Article
- Comprehensive Review of L-Lysine: Chemistry, Occurrence, and Physiological Roles.Current protein & peptide science · 2026Review
- TK2268 encodes the major aminotransferase involved in the conversion from oxaloacetic acid to aspartic acid inApplied and environmental microbiology · 2025Article
- Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function.FEBS letters · 2025Article
- An energy-conserving reaction in amino acid metabolism catalyzed by arginine synthetase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- 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
- Electrostatic Ratchet for Successive Peptide Synthesis in Nonribosomal Molecular Machine RimK.Journal of the American Chemical Society · 2023Article
- Structural insights into the mechanism of adaptive ribosomal modification by Pseudomonas RimK.Proteins · 2023Article
- Thermo-L-Asparaginases: From the Role in the Viability of Thermophiles and Hyperthermophiles at High Temperatures to a Molecular Understanding of Their Thermoactivity and Thermostability.International journal of molecular sciences · 2023Review
- Interconnected Set of Enzymes Provide Lysine Biosynthetic Intermediates and Ornithine Derivatives as Key Precursors for the Biosynthesis of Bioactive Secondary Metabolites.Antibiotics (Basel, Switzerland) · 2023Review
- Biochemical and genetic examination of two aminotransferases from the hyperthermophilic archaeonFrontiers in microbiology · 2023Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- Ancestral state reconstruction of metabolic pathways across pangenome ensembles.Microbial genomics · 2020Article
- An overview of 25 years of research on Thermococcus kodakarensis, a genetically versatile model organism for archaeal research.Folia microbiologica · 2020Review
- Structural polymorphism of the Escherichia coli poly-α-L-glutamate synthetase RimK.Acta crystallographica. Section F, Structural biology communications · 2018Article
- An ornithine ω-aminotransferase required for growth in the absence of exogenous proline in the archaeonThe Journal of biological chemistry · 2018Article
- Evolutionary convergence in the biosyntheses of the imidazole moieties of histidine and purines.PloS one · 2018Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We recently discovered a biosynthetic system using a novel amino group carrier protein called LysW for lysine biosynthesis via α-aminoadipate (AAA), and revealed that this system is also utilized in the biosynthesis of arginine by Sulfolobus In the present study, we focused on the biosynthesis of lysine and ornithine in the hyperthermophilic archaeon Thermococcus kodakarensis, and showed that their biosynthesis is accomplished by a single set of metabolic enzymes. We also determined the crystal structure of the LysX family protein from T. kodakarensis, which catalyzes the conjugation of LysW with either AAA or glutamate, in a complex with LysW-γ-AAA. This crystal structure is the first example to show how LysX recognizes AAA as a substrate and provides a structural basis for the bifunctionality of the LysX family protein from T. kodakarensis Based on comparisons with other LysX family proteins, we propose a mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities.
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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.