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    AADAT aminoadipate aminotransferase [ Homo sapiens (human) ]

    Gene ID: 51166, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Expression analysis of selected genes involved in tryptophan metabolic pathways in Egyptian children with Autism Spectrum Disorder and learning disabilities.

    Expression analysis of selected genes involved in tryptophan metabolic pathways in Egyptian children with Autism Spectrum Disorder and learning disabilities.
    Higazi AM, Kamel HM, Abdel-Naeem EA, Abdullah NM, Mahrous DM, Osman AM., Free PMC Article

    10/30/2021
    N-Acetylcysteine Inhibits Kynurenine Aminotransferase II.

    N-Acetylcysteine Inhibits Kynurenine Aminotransferase II.
    Blanco-Ayala T, Sathyasaikumar KV, Uys JD, Pérez-de-la-Cruz V, Pidugu LS, Schwarcz R., Free PMC Article

    06/19/2021
    In this work, we assessed the relationship between single-nucleotide polymorphisms (SNPs) of KAT1, KAT2 and IDO1 gene encoding, and the risk of depression development. Our study was performed on the DNA isolated from peripheral blood of 281 depressed patients and 236 controls. We genotyped, by using TaqMan probes, four polymorphism.

    Variation of genes encoding KAT1, AADAT and IDO1 as a potential risk of depression development.
    Wigner P, Czarny P, Synowiec E, Bijak M, Talarowska M, Galecki P, Szemraj J, Sliwinski T.

    02/23/2019
    The free thyroxine(FT4)-associated variant rs6854291-influences transcript levels of kynurenine/alpha-aminoadipate aminotransferase (AADAT) in thyroid, implicating AADAT as the causal gene underlying the FT4 association at this locus. AADAT-rs6854291 is associated with both the 3,3',5-triiodothyronine (T3) levels and T3/T4 ratio.

    Genome-wide analyses identify a role for SLC17A4 and AADAT in thyroid hormone regulation.
    Teumer A, Chaker L, Groeneweg S, Li Y, Di Munno C, Barbieri C, Schultheiss UT, Traglia M, Ahluwalia TS, Akiyama M, Appel EVR, Arking DE, Arnold A, Astrup A, Beekman M, Beilby JP, Bekaert S, Boerwinkle E, Brown SJ, De Buyzere M, Campbell PJ, Ceresini G, Cerqueira C, Cucca F, Deary IJ, Deelen J, Eckardt KU, Ekici AB, Eriksson JG, Ferrrucci L, Fiers T, Fiorillo E, Ford I, Fox CS, Fuchsberger C, Galesloot TE, Gieger C, Gögele M, De Grandi A, Grarup N, Greiser KH, Haljas K, Hansen T, Harris SE, van Heemst D, den Heijer M, Hicks AA, den Hollander W, Homuth G, Hui J, Ikram MA, Ittermann T, Jensen RA, Jing J, Jukema JW, Kajantie E, Kamatani Y, Kasbohm E, Kaufman JM, Kiemeney LA, Kloppenburg M, Kronenberg F, Kubo M, Lahti J, Lapauw B, Li S, Liewald DCM, Lifelines Cohort Study, Lim EM, Linneberg A, Marina M, Mascalzoni D, Matsuda K, Medenwald D, Meisinger C, Meulenbelt I, De Meyer T, Meyer Zu Schwabedissen HE, Mikolajczyk R, Moed M, Netea-Maier RT, Nolte IM, Okada Y, Pala M, Pattaro C, Pedersen O, Petersmann A, Porcu E, Postmus I, Pramstaller PP, Psaty BM, Ramos YFM, Rawal R, Redmond P, Richards JB, Rietzschel ER, Rivadeneira F, Roef G, Rotter JI, Sala CF, Schlessinger D, Selvin E, Slagboom PE, Soranzo N, Sørensen TIA, Spector TD, Starr JM, Stott DJ, Taes Y, Taliun D, Tanaka T, Thuesen B, Tiller D, Toniolo D, Uitterlinden AG, Visser WE, Walsh JP, Wilson SG, Wolffenbuttel BHR, Yang Q, Zheng HF, Cappola A, Peeters RP, Naitza S, Völzke H, Sanna S, Köttgen A, Visser TJ, Medici M., Free PMC Article

    01/12/2019
    Immunohistochemical analysis revealed the presence of KAT I, II, and III in all examined corneal sections.

    The presence of kynurenine aminotransferases in the human cornea: Evidence from bioinformatics analysis of gene expression and immunohistochemical staining.
    Matysik-Woźniak A, Jünemann A, Turski WA, Wnorowski A, Jóźwiak K, Paduch R, Okuno E, Moneta-Wielgoś J, Chorągiewicz T, Maciejewski R, Rejdak R., Free PMC Article

    04/14/2018
    he optimised method of protein production provides a fast and reliable technique to generate large quantities of active human KAT2 suitable for future small-molecule lead compound screening and structural design work.

    Expression, purification and crystallization of human kynurenine aminotransferase 2 exploiting a highly optimized codon set.
    Sun G, Nematollahi A, Nadvi NA, Kwan AH, Jeffries CM, Church WB.

    12/17/2016
    Participants with major depression had lower levels of kynurenine compared to controls, with intermediate concentrations in somatoform patients.

    Exercise affects symptom severity but not biological measures in depression and somatization - results on IL-6, neopterin, tryptophan, kynurenine and 5-HIAA.
    Hennings A, Schwarz MJ, Riemer S, Stapf TM, Selberdinger VB, Rief W.

    08/8/2015
    Somatization is characterized by disorders in kynurenine aminotransferase activity and an increased neurotoxic potential

    Somatization, but not depression, is characterized by disorders in the tryptophan catabolite (TRYCAT) pathway, indicating increased indoleamine 2,3-dioxygenase and lowered kynurenine aminotransferase activity.
    Maes M, Galecki P, Verkerk R, Rief W.

    09/17/2011
    association of SNP AADAT+401C/T with the host immune response to bacterial meningitis, suggesting that this SNP may affect the host ability in recruitment of leukocytes to the infection site

    Association of kynurenine aminotransferase II gene C401T polymorphism with immune response in patients with meningitis.
    de Souza FR, Fontes FL, da Silva TA, Coutinho LG, Leib SL, Agnez-Lima LF., Free PMC Article

    07/2/2011
    Observational study of gene-disease association. (HuGE Navigator)

    Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
    Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ., Free PMC Article

    12/5/2010
    analysis of the crystal structure of human kynurenine aminotransferase II

    Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia.
    Rossi F, Garavaglia S, Montalbano V, Walsh MA, Rizzi M.

    01/21/2010
    analysis of the crystal structure of kynurenine aminotransferase II

    Crystal structure of human kynurenine aminotransferase II.
    Han Q, Robinson H, Li J.

    01/21/2010
    A human cDNA encodes a 425-residue protein with a mitochondrial cleavage signal and a pyridoxal-phosphate binding site, ~70% identical to the mouse and rat AADAT orthologs. Bacterial expression studies confirm that the gene encodes AADAT activity.

    Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT).
    Goh DL, Patel A, Thomas GH, Salomons GS, Schor DS, Jakobs C, Geraghty MT.

    07/17/2003
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