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Title: Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket

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 Marinobacter aquaeolei VT8 and an additional enzyme from Acinetobacter baylyi were heterologously expressed in Escherichia coli 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. Finally, 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 M. aquaeolei 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. Amore » likely model for how catalysis by the enzyme is accomplished is also provided.« less

Authors:
 [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1];  [1]
  1. Univ. of Minnesota, Minneapolis, MN (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Science Foundation (NSF); National Institutes of Health (NIH); USDOE Office of Science (SC)
OSTI Identifier:
1430302
Grant/Contract Number:  
0968781; CBET-1437758; CHE-1151547; NIGMS R35-GM118047; NIGMS P41-GM103403; S10 RR029205; AC02-06CH11357
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Applied and Environmental Microbiology
Additional Journal Information:
Journal Volume: 83; Journal Issue: 12; Journal ID: ISSN 0099-2240
Publisher:
American Society for Microbiology
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; Marinobacter; Maqu_3316; decanal; wax ester; lipid biosynthesis

Citation Formats

Bertram, Jonathan H., Mulliner, Kalene M., Shi, Ke, Plunkett, Mary H., Nixon, Peter, Serratore, Nicholas A., Douglas, Christopher J., Aihara, Hideki, and Barney, Brett M. Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket. United States: N. p., 2017. Web. doi:10.1128/AEM.00018-17.
Bertram, Jonathan H., Mulliner, Kalene M., Shi, Ke, Plunkett, Mary H., Nixon, Peter, Serratore, Nicholas A., Douglas, Christopher J., Aihara, Hideki, & Barney, Brett M. Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket. United States. doi:10.1128/AEM.00018-17.
Bertram, Jonathan H., Mulliner, Kalene M., Shi, Ke, Plunkett, Mary H., Nixon, Peter, Serratore, Nicholas A., Douglas, Christopher J., Aihara, Hideki, and Barney, Brett M. Fri . "Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket". United States. doi:10.1128/AEM.00018-17. https://www.osti.gov/servlets/purl/1430302.
@article{osti_1430302,
title = {Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket},
author = {Bertram, Jonathan H. and Mulliner, Kalene M. and Shi, Ke and Plunkett, Mary H. and Nixon, Peter and Serratore, Nicholas A. and Douglas, Christopher J. and Aihara, Hideki and Barney, Brett M.},
abstractNote = {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 Marinobacter aquaeolei VT8 and an additional enzyme from Acinetobacter baylyi were heterologously expressed in Escherichia coli 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. Finally, 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 M. aquaeolei 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.},
doi = {10.1128/AEM.00018-17},
journal = {Applied and Environmental Microbiology},
issn = {0099-2240},
number = 12,
volume = 83,
place = {United States},
year = {2017},
month = {4}
}

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