TL;DR: The plant epimerase undergoes a complex regulation and could control the carbon flux into the vitamin C pathway in response to the redox state of the cell, stress conditions, and GDP-sugar demand for the cell wall/glycoprotein biosynthesis.
TL;DR: The direct demonstration of AREspecific binding protein activity localized to the NAD+-binding region of GAPDH supports the general concept that enzymes containing this domain may exhibit specific RNA binding activity and play additional roles in nucleic acid metabolism.
TL;DR: Two crystal structures of a SIR2 homolog from Archaeoglobus fulgidus complexed with NAD have been determined and provide important insights into the catalytic mechanism of NAD-dependent protein deacetylation by this family of enzymes.
TL;DR: Sequence comparisons of the class 3 ALDH with other ALDHs indicate a similar polypeptide fold, novel NAD-binding mode and catalytic site for this family, and a mechanism for enzymatic specificity and activity is postulated.
Abstract: The first structure of an aldehyde dehydrogenase (ALDH) is described at 2.6 A resolution. Each subunit of the dimeric enzyme contains an NAD-binding domain, a catalytic domain and a bridging domain. At the interface of these domains is a 15 A long funnel-shaped passage with a 6 × 12 A opening leading to a putative catalytic pocket. A new mode of NAD binding, which differs substantially from the classic β-α-β binding mode associated with the ‘Rossmann fold’, is observed which we term the β-α,β mode. Sequence comparisons of the class 3 ALDH with other ALDHs indicate a similar polypeptide fold, novel NAD-binding mode and catalytic site for this family. A mechanism for enzymatic specificity and activity is postulated.
TL;DR: The crystal structure of lobster d -glyceraldehyde-3-phosphate dehydrogenase has been analyzed and it is shown that the amino acids in the active center region and involved in subunit-subunit contacts are more highly conserved than other residues.