| Type: | Family | Name: | 6-phosphogluconate dehydrogenase |
| Description: | This entry represents prokaryotic and eukaryotic 6PGD and a truncated prokaryotic 6PGD that lacks of a central region of about 140 residues, such as yqeC from Bacillus subtilis []. Bacillus subtilis contains three classes of 6-phosphogluconate dehydrogenases (6PGD), including Gnd (YqjI), GntZ and YqeC. All of them are included in this entry. YgjiI is NADP+ dependent, while GntZ and YqeC are NAD+-dependent []. 6-Phosphogluconate dehydrogenase () (6PGD) is a key enzyme that produces NADPH by converting 6-phospho D-gluconolactone to D-ribulose 5-phosphate in the pentose phosphate pathways (PPP) [, ]. NADPH provides the major reducing power required for lipid production and protecting the cell against oxidative stress. 6PGD has been extensively studied with respect to kinetics, regulation, role in pentose-shunt production of NADPH and lipogenesis, and population genetics []. 6PGD is associated with several human disorders including cancer and Alzheimer's disease. The structure of the budding yeast 6PGD (also known as Gnd1) has been revealed []. Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequence are highly conserved []. The protein is a homodimer in which the monomers act independently []: each contains a large, mainly alpha-helical domain and a smaller beta-alpha-beta domain, containing a mixed parallel and anti-parallel 6-stranded beta sheet [, ]. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket []. | Short Name: | Pgluconate_DH |
