Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA258430 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:NHLBI TOPMed: Genetic Epidemiology Network of Salt-Sensitivity (GenSalt)
| PRJNA343579 | ENA
Project description:Genetic Epidemiology Network of Salt Sensitivity (GenSalt)
| PRJNA258429 | ENA
Project description:NHLBI TOPMed: Genetic Epidemiology Network of Salt-Sensitivity (GenSalt)
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Project description:Genetic Epidemiology Network of Arteriopathy (GENOA)
| PRJNA352447 | ENA
Project description:To study pathways associated with ferroptosis sensitivity
2022-06-01 | GSE173905 | GEO
Project description:STAMPEED: Genetic Epidemiology Network of Arteriopathy (GENOA)
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Project description:Genetic Epidemiology Network of Arteriopathy (GENOA): GWAS Studies
| PRJNA393229 | ENA
Project description:NHLBI TOPMed: Genetic Epidemiology Network of Arteriopathy (GENOA)
| PRJNA381260 | ENA
Project description: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.
| S-EPMC2531291 | biostudies-literature
Project description:<p>The GenSalt study aims to identify genes which interact with dietary sodium and potassium intake to influence blood pressure in Han Chinese participants from rural north China. Whole genome sequencing will be conducted among 1,860 participants of the Genetic Epidemiology Network of Salt Sensitivity (GenSalt) Study. We will work in collaboration with participating TOPMed studies to identify novel common, low-frequency and rare variants associated with an array of cardiometabolic phenotypes. In addition, we will explore the relation of low-frequency and rare variants with salt-sensitivity among GenSalt study participants.</p>
| phs001217 | dbGaP