2E1M

Crystal Structure of L-Glutamate Oxidase from Streptomyces sp. X-119-6

2E1M の概要

• エントリーDOI: 10.2210/pdb2e1m/pdb
• 分子名称: L-glutamate oxidase, PHOSPHATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: l-amino acid oxidase, l-glutamate oxidase, fad, l-gox, flavoprotein, oxidoreductase
• 由来する生物種: Streptomyces sp.; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 77501.60

構造登録者

Sasaki, C.,Kashima, A.,Sakaguchi, C.,Mizuno, H.,Arima, J.,Kusakabe, H.,Tamura, T.,Sugio, S.,Inagaki, K. (登録日: 2006-10-26, 公開日: 2007-11-13, 最終更新日: 2023-10-25)

主引用文献

Arima, J.,Sasaki, C.,Sakaguchi, C.,Mizuno, H.,Tamura, T.,Kashima, A.,Kusakabe, H.,Sugio, S.,Inagaki, K.
Structural characterization of l-glutamate oxidase from Streptomyces sp. X-119-6
Febs J., 276:4318-4327, 2009

PubMed Abstract: L-Glutamate oxidase (LGOX) from Streptomyces sp. X-119-6, which catalyzes the oxidative deamination of L-glutamate, has attracted increasing attention as a component of amperometric L-glutamate sensors used in the food industry and clinical biochemistry. The precursor of LGOX, which has a homodimeric structure, is less active than the mature enzyme with an alpha(2)beta(2)V(2) structure; enzymatic proteolysis of the precursor forms the stable mature enzyme. We solved the crystal structure of mature LGOX using molecular replacement with a structurally homologous model of L-amino acid oxidase (LAAO) from snake venom: LGOX has a deeply buried active site and two entrances from the surface of the protein into the active site. Comparison of the LGOX structure with that of LAAO revealed that LGOX has three regions that are absent from the LAAO structure, one of which is involved in the formation of the entrance. Furthermore, the arrangement of the residues composing the active site differs between LGOX and LAAO, and the active site of LGOX is narrower than that of LAAO. Results of the comparative analyses described herein raise the possibility that such a unique structure of LGOX is associated with its substrate specificity.

PubMed: 19531050
DOI: 10.1111/j.1742-4658.2009.07103.x

実験手法

X-RAY DIFFRACTION (2.8 Å)