5U0L

X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from Marinobacter aquaeolei VT8 complexed with a substrate

5U0L の概要

• エントリーDOI: 10.2210/pdb5u0l/pdb
• 関連するPDBエントリー: 5U0M
• 分子名称: N-succinylglutamate 5-semialdehyde dehydrogenase, 1,2-ETHANEDIOL, decanal, ... (7 entities in total)
• 機能のキーワード: dehydrogenase, oxidoreductase
• 由来する生物種: Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107755.97

構造登録者

Shi, K.,Mulliner, K.,Barney, B.M.,Aihara, H. (登録日: 2016-11-24, 公開日: 2017-04-26, 最終更新日: 2023-10-04)

主引用文献

Bertram, J.H.,Mulliner, K.M.,Shi, K.,Plunkett, M.H.,Nixon, P.,Serratore, N.A.,Douglas, C.J.,Aihara, H.,Barney, B.M.
Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket.
Appl. Environ. Microbiol., 83:-, 2017

PubMed Abstract: Enzymes involved in lipid biosynthesis and metabolism play an important role in energy conversion and storage and in the function of structural components such as cell membranes. The fatty aldehyde dehydrogenase (FAldDH) plays a central function in the metabolism of lipid intermediates, oxidizing fatty aldehydes to the corresponding fatty acid and competing with pathways that would further reduce the fatty aldehydes to fatty alcohols or require the fatty aldehydes to produce alkanes. In this report, the genes for four putative FAldDH enzymes from VT8 and an additional enzyme from were heterologously expressed in and shown to display FAldDH activity. Five enzymes (Maqu_0438, Maqu_3316, Maqu_3410, Maqu_3572, and the enzyme reported under RefSeq accession no. WP_004927398) were found to act on aldehydes ranging from acetaldehyde to hexadecanal and also acted on the unsaturated long-chain palmitoleyl and oleyl aldehydes. A comparison of the specificities of these enzymes with various aldehydes is presented. Crystallization trials yielded diffraction-quality crystals of one particular FAldDH (Maqu_3316) from VT8. Crystals were independently treated with both the NAD cofactor and the aldehyde substrate decanal, revealing specific details of the likely substrate binding pocket for this class of enzymes. A likely model for how catalysis by the enzyme is accomplished is also provided. This study provides a comparison of multiple enzymes with the ability to oxidize fatty aldehydes to fatty acids and provides a likely picture of how the fatty aldehyde and NAD are bound to the enzyme to facilitate catalysis. Based on the information obtained from this structural analysis and comparisons of specificities for the five enzymes that were characterized, correlations to the potential roles played by specific residues within the structure may be drawn.

PubMed: 28389542
DOI: 10.1128/AEM.00018-17

実験手法

X-RAY DIFFRACTION (2.285 Å)