ArticleBiochemistry2007
Crystal structure of Homo sapiens kynureninase.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- The Tryptophan-Kynurenine Pathway as a Key Mediator of the Gut-Brain Axis in Depression and Alzheimer's Disease.International journal of molecular sciences · 2026Review
- Docking Analysis of Drugs Used in the Treatment of Alzheimer's Disease, Using Cell Membrane Receptors and Enzymes of the Kynurenine Pathway: A Pilot Study.International journal of molecular sciences · 2026Article
- Integrin-binding sialoprotein as an extracellular matrix-associated independent prognostic biomarker in glioma.BMC cancer · 2026Article
- Exercise training restores longevity-associated tryptophan metabolite 3-hydroxyanthranilic acid levels in middle-aged adults.Acta physiologica (Oxford, England) · 2025Article
- Identification and functional validation of kynureninases from oral bacteria.Journal of oral microbiology · 2025Article
- Molecular Insights Into the Interaction of Tryptophan Metabolites With Tryptophan and Indoleamine 2,3-Dioxygenases: Nitric Oxide a New Effector of Tryptophan 2,3-Dioxygenase and Their Roles in Infection.International journal of tryptophan research : IJTR · 2025Article
- Mechanistic conformational and substrate selectivity profiles emerging in the evolution of enzymes via parallel trajectories.Nature communications · 2024Article
- Bypassing evolutionary dead ends and switching the rate-limiting step of a human immunotherapeutic enzyme.Nature catalysis · 2022Article
- The TZM-bl Reporter Cell Line Expresses Kynureninase That Can Neutralize 2F5-like Antibodies in the HIV-1 Neutralization Assay.International journal of molecular sciences · 2022Article
- Kynurenic Acid Acts as a Signaling Molecule Regulating Energy Expenditure and Is Closely Associated With Metabolic Diseases.Frontiers in endocrinology · 2022Review
- New cases that expand the genotypic and phenotypic spectrum of Congenital NAD Deficiency Disorder.Human mutation · 2021Article
- KYNU, a novel potential target that underpins CD44-promoted breast tumour cell invasion.Journal of cellular and molecular medicine · 2021Review
- NADFrontiers in molecular biosciences · 2021Review
- Conformational Dynamics Contribute to Substrate Selectivity and Catalysis in Human Kynureninase.ACS chemical biology · 2020Article
- Pyridoxal 5'-Phosphate-Dependent Enzymes at the Crossroads of Host-Microbe Tryptophan Metabolism.International journal of molecular sciences · 2020Review
- Cysteine catabolism and the serine biosynthesis pathway support pyruvate production during pyruvate kinase knockdown in pancreatic cancer cells.Cancer & metabolism · 2019Article
- [Effect of Arg188Gln (G/A) mutation on enzymatic activity of kynureninase].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2017Article
- Major Developments in the Design of Inhibitors along the Kynurenine Pathway.Current medicinal chemistry · 2017Review
- HIV-1 Envelope Mimicry of Host Enzyme Kynureninase Does Not Disrupt Tryptophan Metabolism.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- General base-general acid catalysis by terpenoid cyclases.The Journal of antibiotics · 2016Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.
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Registered trials
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