Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA95085 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:RECURRENT SETBP1 MUTATIONS IN ATYPICAL CHRONIC MYELOID LEUKEMIA
| PRJNA179284 | ENA
Project description:Whole-exome sequencing of chronic myeloid leukemia
| PRJNA213438 | ENA
Project description:Characterization of miRNomes in acute and chronic myeloid leukemia cells
| PRJNA208839 | ENA
Project description:Discovery of the targets of the immune response to chronic myeloid leukemia in 3 patients using protein microarrays
| PRJNA109145 | ENA
Project description:Epigenomics Studies in Acute Myeloid Leukemia disease progression [RNAseq]
| PRJNA326266 | ENA
Project description:BCL6 is required for the initiation and maintenance of chronic myeloid leukemia
| PRJNA135225 | ENA
Project description:Transcriptome characterization of chronic myeloid leukemia by RNA sequencing
| PRJNA390519 | ENA
Project description:SNP array data for 56 chronic myeloid leukemia samples.
| PRJNA105227 | ENA
Project description:To study pathways associated with ferroptosis sensitivity
2022-06-01 | GSE173905 | GEO
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