5YB7

L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 - L-ornithine complex

5YB7 の概要

• エントリーDOI: 10.2210/pdb5yb7/pdb
• 分子名称: L-amino acid oxidase/monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE, L-ornithine, ... (4 entities in total)
• 機能のキーワード: l-amino acid oxidase/monooxygenase, flavin-containing monoamine oxidase family, flavin monooxygenases, l-ornithine, oxidoreductase
• 由来する生物種: Pseudomonas sp. AIU 813
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 262266.97

構造登録者

Im, D.,Matsui, D.,Arakawa, T.,Isobe, K.,Asano, Y.,Fushinobu, S. (登録日: 2017-09-03, 公開日: 2018-02-07, 最終更新日: 2023-11-22)

主引用文献

Im, D.,Matsui, D.,Arakawa, T.,Isobe, K.,Asano, Y.,Fushinobu, S.
Ligand complex structures of l-amino acid oxidase/monooxygenase from
FEBS Open Bio, 8:314-324, 2018

PubMed Abstract: l-Amino acid oxidase/monooxygenase from sp. AIU 813 (l-AAO/MOG) catalyzes both the oxidative deamination and oxidative decarboxylation of the α-group of l-Lys to produce a keto acid and amide, respectively. l-AAO/MOG exhibits limited specificity for l-amino acid substrates with a basic side chain. We previously determined its ligand-free crystal structure and identified a key residue for maintaining the dual activities. Here, we determined the structures of l-AAO/MOG complexed with l-Lys, l-ornithine, and l-Arg and revealed its substrate recognition. Asp238 is located at the ceiling of a long hydrophobic pocket and forms a strong interaction with the terminal, positively charged group of the substrates. A mutational analysis on the D238A mutant indicated that the interaction is critical for substrate binding but not for catalytic control between the oxidase/monooxygenase activities. The catalytic activities of the D238E mutant unexpectedly increased, while the D238F mutant exhibited altered substrate specificity to long hydrophobic substrates. In the ligand-free structure, there are two channels connecting the active site and solvent, and a short region located at the dimer interface is disordered. In the l-Lys complex structure, a loop region is displaced to plug the channels. Moreover, the disordered region in the ligand-free structure forms a short helix in the substrate complex structures and creates the second binding site for the substrate. It is assumed that the amino acid substrate enters the active site of l-AAO/MOG through this route.

PubMed: 29511608
DOI: 10.1002/2211-5463.12387

実験手法

X-RAY DIFFRACTION (2 Å)