Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA75353 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Exome Sequencing in Autosomal Recessive Progressive External Ophthalmoplegia
| PRJNA75351 | ENA
Project description:Autosomal recessive TPPII mutations cause a new human immunodeficiency
| PRJNA269324 | ENA
Project description:<p>Progressive external ophthalmoplegia (PEO) is an inherited mitochondrial disease that follows either autosomal dominant or recessive forms of inheritance (adPEO or arPEO). AdPEO is a genetically heterogeneous disease and several genes including <i>POLG1</i> and <i>C10orf2</i>/Twinkle have been identified as responsible genes. On the other hand, <i>POLG1</i> was the only established gene causing arPEO with mitochondrial DNA deletions. We previously reported a case of PEO with unidentified genetic etiology. The patient was born of a first-cousin marriage. Therefore, the recessive form of inheritance was suspected. To identify the disease causing variant in this patient, we subjected the patient's DNA to whole-exome sequencing and narrowed down the candidate variants using public data and runs of homozygosity analysis.</p>
| phs000392 | dbGaP
Project description:Susceptibility to respiratory infections due to autosomal recessive IFIH1 mutations
| PRJNA351275 | 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:RNA extracted at 240min. Samples are rRNA depleted. Expression measurement of Homo sapiens genes.
2019-07-31 | GSE114179 | GEO
Project description:Autosomal recessive PGM3 mutations cause a new Congenital Disorder of Glycosylation
| PRJNA262959 | ENA
Project description:Autosomal recessive PGM3 mutations cause a new Congenital Disorder of Glycosylation
| PRJNA262960 | ENA
Project description:Identification of autosomal recessive spastic paraplegia with cerebellar ataxia and neuropathy
| PRJDB2708 | ENA