Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 83, Issue 12, Pages -Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.00018-17
Keywords
Marinobacter; Maqu_3316; decanal; wax ester; lipid biosynthesis
Categories
Funding
- National Science Foundation [0968781, CBET-1437758, CHE-1151547]
- National Institutes of Health [NIGMS R35-GM118047]
- University of Minnesota
- U.S. National Institutes of Health [NIGMS P41-GM103403]
- NIH-ORIP HEI [S10 RR029205]
- Argonne National Laboratory [DE-AC02-06CH11357]
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [1437758] Funding Source: National Science Foundation
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1151547] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0968781] Funding Source: National Science Foundation
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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. 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. IMPORTANCE 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.
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