| Gene Ontology | |
|---|---|
| Molecular function | • phosphoglycerate dehydrogenase activity • electron carrier activity • NAD binding |
| Cellular component | • cytosol |
| Biological process | • glutamine metabolic process • glycine metabolic process • L-serine biosynthetic process • threonine metabolic process • brain development • cellular amino acid biosynthetic process • gamma-aminobutyric acid metabolic process • regulation of gene expression • taurine metabolic process • spinal cord development • glial cell development • neural tube development • cell cycle process • neuron projection development • cellular nitrogen compound metabolic process • small molecule metabolic process |
| Sources: Amigo / QuickGO | |
120.2 – 120.29 Mb
98.31 – 98.34 Mb
| phosphoglycerate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.95 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | |||||||||
In enzymology, a D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95) is an enzyme that catalyzes the chemical reactions
Thus, in the first case, the two substrates of this enzyme are 3-phospho-D-glycerate and NAD+, whereas its 3 products are 3-phosphonooxypyruvate, NADH, and H+; in the second case, the two substrates of this enzyme are 2-hydroxyglutarate and NAD+, whereas its 3 products are 2-oxoglutarate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. In humans, this enzyme is encoded by the PHGDH gene. 3-Phosphoglycerate dehydrogenase (PHGDH; EC 1.1.1.95) catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first and rate-limiting step in the phosphorylated pathway of serine biosynthesis, using NAD+/NADH as a cofactor. Certain breast cancers are dependent on the overexpression of PHGDH. | |||||||||