Ontology highlight
ABSTRACT:
SUBMITTER: Korasick DA
PROVIDER: S-EPMC6188814 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature
Korasick David A DA White Tommi A TA Chakravarthy Srinivas S Tanner John J JJ
FEBS letters 20180918 19
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<sup>+</sup> -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 ...[more]