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Title: SAXS fingerprints of aldehyde dehydrogenase oligomers

Publication Date:
Sponsoring Org.:
OSTI Identifier:
Grant/Contract Number:
AC02-05CH11231; R01GM105404
Resource Type:
Journal Article: Published Article
Journal Name:
Data in Brief
Additional Journal Information:
Journal Volume: 5; Journal Issue: C; Related Information: CHORUS Timestamp: 2017-09-16 03:34:22; Journal ID: ISSN 2352-3409
Country of Publication:
United States

Citation Formats

Tanner, John J. SAXS fingerprints of aldehyde dehydrogenase oligomers. United States: N. p., 2015. Web. doi:10.1016/j.dib.2015.10.017.
Tanner, John J. SAXS fingerprints of aldehyde dehydrogenase oligomers. United States. doi:10.1016/j.dib.2015.10.017.
Tanner, John J. Tue . "SAXS fingerprints of aldehyde dehydrogenase oligomers". United States. doi:10.1016/j.dib.2015.10.017.
title = {SAXS fingerprints of aldehyde dehydrogenase oligomers},
author = {Tanner, John J.},
abstractNote = {},
doi = {10.1016/j.dib.2015.10.017},
journal = {Data in Brief},
number = C,
volume = 5,
place = {United States},
year = {Tue Dec 01 00:00:00 EST 2015},
month = {Tue Dec 01 00:00:00 EST 2015}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1016/j.dib.2015.10.017

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  • 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 fromMarinobacter aquaeoleiVT8 and an additional enzyme fromAcinetobacter baylyiwere heterologously expressed inEscherichia coliand shown to display FAldDH activity.more » 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) fromM. aquaeoleiVT8. 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. IMPORTANCEThis 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.« less
  • Polyetherurethane oligomers with aldehyde groups, which we synthesized from polyoxypropylene diols (molecular weight 500, 1000, 1500, 2000, or 3000) with toluene diisocyanate and salicylaldehyde, are of interest as additives for lubricating oils. The effects of these oligomers on the service properties and physicochemical characteristics of lubricating oils were investigated by methods prreviously described. As the lube base stocks we used castor oil, a polyoxypropylene diol and a polyethoxysiloxane. The oligomers are readily soluble in organic solvents and in the lube base stocks, and their solutions are stable during storage and use. We found that the optimal concentration of oligomers ismore » 5%, providing the best lubricating properties, in particular the best antiwear properties.« less
  • A coenzyme A (CoA)-acylating aldehyde dehydrogenase (ALDH), which also converts acyl-CoA to aldehyde and CoA, has been purified under anaerobic conditions from Clostridium beijerinckii NRRL B592. The ALDH showed a native molecular weight (M{sub r}) of 100,000 and a subunit M{sub r} of 55,000, suggesting that ALDH is dimeric. Purified ALDH contained no alcohol dehydrogenase activity. Activities measured with acetaldehyde and butyraldehyde as alternative substrates were copurified, indicating that the same ALDH can catalyze the formation of both aldehydes for ethanol and butanol production. Based on the K{sub m} and V{sub max} values for acetyl-CoA and butyryl-CoA, ALDH was moremore » effective for the production of butyraldehyde than for acetaldehyde. ALDH could use either NAD(H) or NADP(H) as the coenzyme, but the K{sub m} for NAD(H) was much lower than that for NADP(H). Kinetic data suggest a ping-pong mechanism for the reaction. ALDH was more stable in Tris buffer than in phosphate buffer. The apparent optimum pH was between 6.5 and 7 for the forward reaction (the physiological direction; aldehyde forming), and it was 9.5 or higher for the reverse reaction (acyl-CoA forming). The ratio of NAD(H)/NADP(H)-linked activities increased with decreasing pH. ALDH was O{sub 2} sensitive, but it could be protected against O{sub 2} inactivation by dithiothreitol. The O{sub 2}-inactivated enzyme could be reactivated by incubating the enzyme with CoA in the presence or absence of dithiothreitol prior to assay.« less