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- SASDD49: High load concentration of apo alpha-aminoadipic semialdehyde deh... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDD49 |
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![]() | High load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS
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Function / homology | ![]() L-aminoadipate-semialdehyde dehydrogenase / L-aminoadipate-semialdehyde dehydrogenase activity / Choline catabolism / choline catabolic process / betaine-aldehyde dehydrogenase / betaine-aldehyde dehydrogenase (NAD+) activity / Lysine catabolism / cellular aldehyde metabolic process / glycine betaine biosynthetic process from choline / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity ...L-aminoadipate-semialdehyde dehydrogenase / L-aminoadipate-semialdehyde dehydrogenase activity / Choline catabolism / choline catabolic process / betaine-aldehyde dehydrogenase / betaine-aldehyde dehydrogenase (NAD+) activity / Lysine catabolism / cellular aldehyde metabolic process / glycine betaine biosynthetic process from choline / glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity / aldehyde dehydrogenase (NAD+) / aldehyde dehydrogenase (NAD+) activity / sensory perception of sound / mitochondrial matrix / mitochondrion / extracellular exosome / identical protein binding / nucleus / cytosol Similarity search - Function |
Biological species | ![]() |
![]() | ![]() Title: NAD promotes assembly of the active tetramer of aldehyde dehydrogenase 7A1. Authors: David A Korasick / Tommi A White / Srinivas Chakravarthy / John J Tanner / ![]() Abstract: Nicotinamide adenine dinucleotide (NAD) is the redox cofactor of many enzymes, including the vast aldehyde dehydrogenase (ALDH) superfamily. Although the function of NAD(H) in hydride transfer is ...Nicotinamide adenine dinucleotide (NAD) is the redox cofactor of many enzymes, including the vast aldehyde dehydrogenase (ALDH) superfamily. Although the function of NAD(H) in hydride transfer is established, its influence on protein structure is less understood. Herein, we show that NAD -binding promotes assembly of the ALDH7A1 tetramer. Multiangle light scattering, small-angle X-ray scattering, and sedimentation velocity all show a pronounced shift of the dimer-tetramer equilibrium toward the tetramer when NAD is present. Furthermore, electron microscopy shows that cofactor binding enhances tetramer formation even at the low enzyme concentration used in activity assays, suggesting the tetramer is the active species. Altogether, our results suggest that the catalytically active oligomer of ALDH7A1 is assembled on demand in response to cofactor availability. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #2114 | ![]() Type: atomic / Chi-square value: 1.73317526915 ![]() |
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Model #2115 | ![]() Type: atomic / Chi-square value: 1.1843605618 ![]() |
Model #2116 | ![]() Type: atomic / Chi-square value: 1.1843605618 ![]() |
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Sample
![]() | Name: High load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS |
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Buffer | Name: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol / pH: 7.8 |
Entity #1150 | Name: ALDH7A1 / Type: protein / Description: Alpha-aminoadipic semialdehyde dehydrogenase / Formula weight: 55.56 / Num. of mol.: 4 / Source: Homo sapiens / References: UniProt: P49419 Sequence: GHMSTLLINQ PQYAWLKELG LREENEGVYN GSWGGRGEVI TTYCPANNEP IARVRQASVA DYEETVKKAR EAWKIWADIP APKRGEIVRQ IGDALREKIQ VLGSLVSLEM GKILVEGVGE VQEYVDICDY AVGLSRMIGG PILPSERSGH ALIEQWNPVG LVGIITAFNF ...Sequence: GHMSTLLINQ PQYAWLKELG LREENEGVYN GSWGGRGEVI TTYCPANNEP IARVRQASVA DYEETVKKAR EAWKIWADIP APKRGEIVRQ IGDALREKIQ VLGSLVSLEM GKILVEGVGE VQEYVDICDY AVGLSRMIGG PILPSERSGH ALIEQWNPVG LVGIITAFNF PVAVYGWNNA IAMICGNVCL WKGAPTTSLI SVAVTKIIAK VLEDNKLPGA ICSLTCGGAD IGTAMAKDER VNLLSFTGST QVGKQVGLMV QERFGRSLLE LGGNNAIIAF EDADLSLVVP SALFAAVGTA GQRCTTARRL FIHESIHDEV VNRLKKAYAQ IRVGNPWDPN VLYGPLHTKQ AVSMFLGAVE EAKKEGGTVV YGGKVMDRPG NYVEPTIVTG LGHDASIAHT ETFAPILYVF KFKNEEEVFA WNNEVKQGLS SSIFTKDLGR IFRWLGPKGS DCGIVNVNIP TSGAEIGGAF GGEKHTGGGR ESGSDAWKQY MRRSTCTINY SKDLPLAQGI KFQ |
-Experimental information
Beam | Instrument name: Advanced Photon Source (APS) BioCAT 18ID / City: Argonne, IL / 国: USA ![]() | ||||||||||||||||||||||||
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Detector | Name: Pilatus 100K / Pixsize x: 172 mm | ||||||||||||||||||||||||
Scan | Measurement date: Feb 22, 2018 / Cell temperature: 22 °C / Exposure time: 0.5 sec. / Unit: 1/A /
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Result | Type of curve: sec Comments: Column type: Wyatt WTC 030 S5; flow rate: 0.8 mL/min; injection volume: 250 - 500 µL
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