SAXS fingerprints of aldehyde dehydrogenase oligomers
Enzymes of the aldehyde dehydrogenase (ALDH) superfamily catalyze the nicotinamide adenine dinucleotide-dependent oxidation of aldehydes to carboxylic acids. ALDHs are important in detoxification of aldehydes, amino acid metabolism, embryogenesis and development, neurotransmission, oxidative stress,...
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| Format: | Article |
| Language: | English |
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Elsevier
2015-12-01
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| Series: | Data in Brief |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340915002656 |
| _version_ | 1818524964521771008 |
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| author | John J. Tanner |
| author_facet | John J. Tanner |
| author_sort | John J. Tanner |
| collection | DOAJ |
| description | Enzymes of the aldehyde dehydrogenase (ALDH) superfamily catalyze the nicotinamide adenine dinucleotide-dependent oxidation of aldehydes to carboxylic acids. ALDHs are important in detoxification of aldehydes, amino acid metabolism, embryogenesis and development, neurotransmission, oxidative stress, and cancer. Mutations in genes encoding ALDHs cause metabolic disorders, including alcohol flush reaction (ALDH2), Sjögren–Larsson syndrome (ALDH3A2), hyperprolinemia type II (ALDH4A1), γ-hydroxybutyric aciduria (ALDH5A1), methylmalonic aciduria (ALDH6A1), pyridoxine dependent epilepsy (ALDH7A1), and hyperammonemia (ALDH18A1). We previously reported crystal structures and small-angle X-ray scattering (SAXS) analyses of ALDHs exhibiting dimeric, tetrameric, and hexameric oligomeric states (Luo et al., Biochemistry 54 (2015) 5513–5522; Luo et al., J. Mol. Biol. 425 (2013) 3106–3120). Herein I provide the SAXS curves, radii of gyration, and distance distribution functions for the three types of ALDH oligomer. The SAXS curves and associated analysis provide diagnostic fingerprints that allow rapid identification of the type of ALDH oligomer that is present in solution. The data sets provided here serve as a benchmark for characterizing oligomerization of ALDHs. |
| first_indexed | 2024-12-11T06:03:36Z |
| format | Article |
| id | doaj.art-b8f139333bf349bb9461c069aa0f938c |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-11T06:03:36Z |
| publishDate | 2015-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-b8f139333bf349bb9461c069aa0f938c2022-12-22T01:18:23ZengElsevierData in Brief2352-34092015-12-015C74575110.1016/j.dib.2015.10.017SAXS fingerprints of aldehyde dehydrogenase oligomersJohn J. TannerEnzymes of the aldehyde dehydrogenase (ALDH) superfamily catalyze the nicotinamide adenine dinucleotide-dependent oxidation of aldehydes to carboxylic acids. ALDHs are important in detoxification of aldehydes, amino acid metabolism, embryogenesis and development, neurotransmission, oxidative stress, and cancer. Mutations in genes encoding ALDHs cause metabolic disorders, including alcohol flush reaction (ALDH2), Sjögren–Larsson syndrome (ALDH3A2), hyperprolinemia type II (ALDH4A1), γ-hydroxybutyric aciduria (ALDH5A1), methylmalonic aciduria (ALDH6A1), pyridoxine dependent epilepsy (ALDH7A1), and hyperammonemia (ALDH18A1). We previously reported crystal structures and small-angle X-ray scattering (SAXS) analyses of ALDHs exhibiting dimeric, tetrameric, and hexameric oligomeric states (Luo et al., Biochemistry 54 (2015) 5513–5522; Luo et al., J. Mol. Biol. 425 (2013) 3106–3120). Herein I provide the SAXS curves, radii of gyration, and distance distribution functions for the three types of ALDH oligomer. The SAXS curves and associated analysis provide diagnostic fingerprints that allow rapid identification of the type of ALDH oligomer that is present in solution. The data sets provided here serve as a benchmark for characterizing oligomerization of ALDHs.http://www.sciencedirect.com/science/article/pii/S2352340915002656Small-angle X-ray scatteringX-ray crystallographyAldehyde dehydrogenaseProtein oligomeric state |
| spellingShingle | John J. Tanner SAXS fingerprints of aldehyde dehydrogenase oligomers Data in Brief Small-angle X-ray scattering X-ray crystallography Aldehyde dehydrogenase Protein oligomeric state |
| title | SAXS fingerprints of aldehyde dehydrogenase oligomers |
| title_full | SAXS fingerprints of aldehyde dehydrogenase oligomers |
| title_fullStr | SAXS fingerprints of aldehyde dehydrogenase oligomers |
| title_full_unstemmed | SAXS fingerprints of aldehyde dehydrogenase oligomers |
| title_short | SAXS fingerprints of aldehyde dehydrogenase oligomers |
| title_sort | saxs fingerprints of aldehyde dehydrogenase oligomers |
| topic | Small-angle X-ray scattering X-ray crystallography Aldehyde dehydrogenase Protein oligomeric state |
| url | http://www.sciencedirect.com/science/article/pii/S2352340915002656 |
| work_keys_str_mv | AT johnjtanner saxsfingerprintsofaldehydedehydrogenaseoligomers |