5AZ0

Crystal structure of aldo-keto reductase (AKR2E5) of the silkworm, Bombyx mori

5AZ0 の概要

• エントリーDOI: 10.2210/pdb5az0/pdb
• 関連するPDBエントリー: 5AZ0
• 分子名称: Uncharacterized protein, CALCIUM ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: enzyme specificity, lepidoptera, oxidoreductase
• 由来する生物種: Bombyx mori (Silk moth)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40418.47

構造登録者

Yamamoto, K.,Higashiura, A.,Suzuki, M.,Nakagawa, A. (登録日: 2015-09-15, 公開日: 2016-02-10, 最終更新日: 2024-03-20)

主引用文献

Yamamoto, K.,Higashiura, A.,Suzuki, M.,Shiotsuki, T.,Sugahara, R.,Fujii, T.,Nakagawa, A.
Structural characterization of an aldo-keto reductase (AKR2E5) from the silkworm Bombyx mori
Biochem.Biophys.Res.Commun., 474:104-110, 2016

PubMed Abstract: We report a new member of the aldo-keto reductase (AKR) superfamily in the silkworm Bombyx mori. Based on its amino acid sequence, the new enzyme belongs to the AKR2 family and was previously assigned the systematic name AKR2E5. In the present study, recombinant AKR2E5 was expressed, purified to homogeneity, and characterized. The X-ray crystal structures were determined at 2.2 Å for the apoenzyme and at 2.3 Å resolution for the NADPH-AKR2E5 complex. Our results demonstrate that AKR2E5 is a 40-kDa monomer and includes the TIM- or (β/α)8-barrel typical for other AKRs. We found that AKR2E5 uses NADPH as a cosubstrate to reduce carbonyl compounds such as DL-glyceraldehyde, xylose, 3-hydroxy benzaldehyde, 17α-hydroxy progesterone, 11-hexadecenal, and bombykal. No NADH-dependent activity was detected. Site-directed mutagenesis of AKR2E5 indicates that amino acid residues Asp70, Tyr75, Lys104, and His137 contribute to catalytic activity, which is consistent with the data on other AKRs. To the best of our knowledge, AKR2E5 is only the second AKR characterized in silkworm. Our data should contribute to further understanding of the functional activity of insect AKRs.

PubMed: 27103441
DOI: 10.1016/j.bbrc.2016.04.079

実験手法

X-RAY DIFFRACTION (2.2 Å)