| Description | 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 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 α-helical domain and a smaller β-α-β domain, containing a mixed parallel and anti-parallel 6-stranded β sheet [, ]. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket [].Bacillus subtilis contains three classes of 6-phosphogluconate dehydrogenases (6PGD), including Gnd (YqjI), GntZ and YqeC (truncated 6PGD). Gnd (YqjI) and GntZ are included in this entry. YgjiI is NADP+ dependent, while GntZ and YqeC are NAD+-dependent [ ]. | Name | 6-phosphogluconate dehydrogenase, decarboxylating |
| Short Name | 6PGDH_Gnd/GntZ | Type | Family |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
