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TitleNAD promotes assembly of the active tetramer of aldehyde dehydrogenase 7A1.
Journal, issue, pagesFEBS Lett, Vol. 592, Issue 19, Page 3229-3238, Year 2018
Publish dateSep 18, 2018
AuthorsDavid A Korasick / Tommi A White / Srinivas Chakravarthy / John J Tanner /
PubMed AbstractNicotinamide 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.
External linksFEBS Lett / PubMed:30184263 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDD29:
Low load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS
Method: SAXS/SANS

SASDD39:
Medium load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS
Method: SAXS/SANS

SASDD49:
High load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS
Method: SAXS/SANS

SASDD59:
Low load concentration of alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS
Method: SAXS/SANS

SASDD69:
Medium load concentration of alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS
Method: SAXS/SANS

SASDD79:
High load concentration of alpha-aminoadipic semialdehyde dehydrogenase ALDH7A1 with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS
Method: SAXS/SANS

Source
  • Homo sapiens (human)

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