5EUN

The Crystal Structure of Human Kynurenine Aminotransferase II, PLP-bound form, at 1.83 A

5EUN の概要

• エントリーDOI: 10.2210/pdb5eun/pdb
• 分子名称: Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (2 entities in total)
• 機能のキーワード: kynurenine aminotransferase ii, llp, transferase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Mitochondrion : Q8N5Z0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47628.55

構造登録者

Nematollahi, A.,Sun, G.,Kwan, A.,Jeffries, C.M.,Harrop, S.J.,Hanrahan, J.R.,Nadvi, N.A.,Church, W.B. (登録日: 2015-11-18, 公開日: 2015-12-16, 最終更新日: 2025-04-02)

主引用文献

Nematollahi, A.,Sun, G.,Harrop, S.J.,Hanrahan, J.R.,Church, W.B.
Structure of the PLP-Form of the Human Kynurenine Aminotransferase II in a Novel Spacegroup at 1.83 angstrom Resolution.
Int J Mol Sci, 17:446-446, 2016

PubMed Abstract: Kynurenine aminotransferase II (KAT-II) is a 47 kDa pyridoxal phosphate (PLP)-dependent enzyme, active as a homodimer, which catalyses the transamination of the amino acids kynurenine (KYN) and 3-hydroxykynurenine (3-HK) in the tryptophan pathway, and is responsible for producing metabolites that lead to kynurenic acid (KYNA), which is implicated in several neurological diseases such as schizophrenia. In order to fully describe the role of KAT-II in the pathobiology of schizophrenia and other brain disorders, the crystal structure of full-length PLP-form hKAT-II was determined at 1.83 Å resolution, the highest available. The electron density of the active site reveals an aldimine linkage between PLP and Lys263, as well as the active site residues, which characterize the fold-type I PLP-dependent enzymes.

PubMed: 27023527
DOI: 10.3390/ijms17040446

実験手法

X-RAY DIFFRACTION (1.825 Å)