| Type: | Family | Name: | D-3-phosphoglycerate dehydrogenase, type2 |
| Description: | Phosphoglycerate dehydrogenases (PGDH) have at least two different structural domains: the nucleotide binding and the substrate binding. There are three types of PGDH: type 3 enzymes are composed only of these two domains, type2 enzymes contain an extra C-terminal regulatory domain (ACT domain), type 1 enzymes contain both the regulatory domain and an extra allosteric domain [, ]. This entry represents the type 2 enzyme. This type of PGDH is found in E. coli and some lower eukaryotes, such as yeast and Neurospora. The type1 PGDH is found in bacteria such as Mycobacterium, Bacillus subtilis, Corynebacterium, plants such as Arabidopsis, and higher order eukaryotes, including mammals []. PGDH catalyses an early step in the biosynthesis of L-serine by converting D-3-phosphoglyceric acid to hydroxypyruvic acid phosphate (HPAP), utilising NAD+ as a coenzyme [, ]. E. coli PGDH is a tetramer made up of four identical subunits []. L-serine binds at the interface between ACT domains and underwent V-type allosteric regulation, which inhibit the enzyme activity []. | Short Name: | PGDH_2 |
