2QLR

Crystal structure of human kynurenine aminotransferase II

2QLR の概要

• エントリーDOI: 10.2210/pdb2qlr/pdb
• 分子名称: Kynurenine/alpha-aminoadipate aminotransferase mitochondrial, GLYCEROL (3 entities in total)
• 機能のキーワード: alpha & beta protein, plp-dependent transferase, aminotransferase, mitochondrion, multifunctional enzyme, pyridoxal phosphate, transit peptide, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion (Potential): Q8N5Z0
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 191619.33

構造登録者

Han, Q.,Robinson, R.,Li, J. (登録日: 2007-07-13, 公開日: 2007-12-04, 最終更新日: 2023-11-15)

主引用文献

Han, Q.,Robinson, H.,Li, J.
Crystal Structure of Human Kynurenine Aminotransferase II
J.Biol.Chem., 283:3567-3573, 2008

PubMed Abstract: Human kynurenine aminotransferase II (hKAT-II) efficiently catalyzes the transamination of knunrenine to kynurenic acid (KYNA). KYNA is the only known endogenous antagonist of N-methyl-D-aspartate (NMDA) receptors and is also an antagonist of 7-nicotinic acetylcholine receptors. Abnormal concentrations of brain KYNA have been implicated in the pathogenesis and development of several neurological and psychiatric diseases in humans. Consequently, enzymes involved in the production of brain KYNA have been considered potential regulatory targets. In this article, we report a 2.16 A crystal structure of hKAT-II and a 1.95 A structure of its complex with kynurenine. The protein architecture of hKAT-II reveals that it belongs to the fold-type I pyridoxal 5-phosphate (PLP)-dependent enzymes. In comparison with all subclasses of fold-type I-PLP-dependent enzymes, we propose that hKAT-II represents a novel subclass in the fold-type I enzymes because of the unique folding of its first 65 N-terminal residues. This study provides a molecular basis for future effort in maintaining physiological concentrations of KYNA through molecular and biochemical regulation of hKAT-II.

PubMed: 18056995
DOI: 10.1074/jbc.M708358200

実験手法

X-RAY DIFFRACTION (2.3 Å)