9ENH

L-amino acid oxidase 4 (HcLAAO4) from the fungus Hebeloma cylindrosporum

9ENH の概要

• エントリーDOI: 10.2210/pdb9enh/pdb
• 関連するPDBエントリー: 9ENI 9ENJ 9ENK 9ENL 9ENM 9ENN
• 分子名称: L-amino acid oxidase 4, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: l-amino acid oxidase, fad, flavoprotein, oxidoreductase
• 由来する生物種: Hebeloma cylindrosporum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 254314.51

構造登録者

Gilzer, D.,Koopmeiners, S.,Fischer von Mollard, G.,Niemann, H.H. (登録日: 2024-03-13, 公開日: 2024-08-14, 最終更新日: 2024-10-09)

主引用文献

Koopmeiners, S.,Gilzer, D.,Widmann, C.,Berelsmann, N.,Spross, J.,Niemann, H.H.,Fischer von Mollard, G.
Crystal structure and enzyme engineering of the broad substrate spectrum l-amino acid oxidase 4 from the fungus Hebeloma cylindrosporum.
Febs Lett., 598:2306-2320, 2024

PubMed Abstract: l-Amino acid oxidases (LAAOs) catalyze the oxidative deamination of l-amino acids to α-keto acids. Recombinant production of LAAOs with broad substrate spectrum remains a formidable challenge. We previously achieved this for the highly active and thermostable LAAO4 of Hebeloma cylindrosporum (HcLAAO4). Here, we crystallized a proteolytically truncated surface entropy reduction variant of HcLAAO4 and solved its structure in substrate-free form and in complex with diverse substrates. The ability to support the aliphatic portion of a substrate's side chain by an overall hydrophobic active site is responsible for the broad substrate spectrum of HcLAAO4, including l-amino acids with big aromatic, acidic and basic side chains. Based on the structural findings, we generated an E288H variant with increased activity toward pharmaceutical building blocks of high interest.

PubMed: 39152524
DOI: 10.1002/1873-3468.15002

実験手法

X-RAY DIFFRACTION (2.3 Å)