Phosphoglycerate dehydrogenase

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Phosphoglycerate dehydrogenase
Protein PHGDH PDB 2g76.png
PDB rendering based on 2g76.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PHGDH ; 3-PGDH; 3PGDH; HEL-S-113; NLS; PDG; PGAD; PGD; PGDH; PHGDHD; SERA
External IDs OMIM606879 MGI1355330 HomoloGene39318 GeneCards: PHGDH Gene
EC number 1.1.1.95
RNA expression pattern
PBB GE PHGDH 201397 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 26227 236539
Ensembl ENSG00000092621 ENSMUSG00000053398
UniProt O43175 Q61753
RefSeq (mRNA) NM_006623 NM_016966
RefSeq (protein) NP_006614 NP_058662
Location (UCSC) Chr 1:
120.2 – 120.29 Mb
Chr 3:
98.31 – 98.34 Mb
PubMed search [1] [2]
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 RCSB PDB PDBe PDBsum

In enzymology, a D-3-phosphoglycerate dehydrogenase (EC 1.1.1.95) is an enzyme that catalyzes the chemical reactions

3-phospho-D-glycerate + NAD+ \rightleftharpoons 3-phosphonooxypyruvate + NADH + H+
2-hydroxyglutarate + NAD+ \rightleftharpoons 2-oxoglutarate + NADH + H+

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.[1] 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.[1] Certain breast cancers are dependent on the overexpression of PHGDH.[2]

Clinical aspect[edit]

Mutations in PHGDH cause Neu-Laxova Syndrome .[3]

References[edit]

  1. ^ a b "Entrez Gene: PHGDH phosphoglycerate dehydrogenase". 
  2. ^ Possemato, Richard; Marks, Kevin M., Shaul, Yoav D., Pacold, Michael E., Kim, Dohoon, Birsoy, Kıvanç, Sethumadhavan, Shalini, Woo, Hin-Koon, Jang, Hyun G., Jha, Abhishek K., Chen, Walter W., Barrett, Francesca G., Stransky, Nicolas, Tsun, Zhi-Yang, Cowley, Glenn S., Barretina, Jordi, Kalaany, Nada Y., Hsu, Peggy P., Ottina, Kathleen, Chan, Albert M., Yuan, Bingbing, Garraway, Levi A., Root, David E., Mino-Kenudson, Mari, Brachtel, Elena F., Driggers, Edward M., Sabatini, David M. (17 August 2011). "Functional genomics reveal that the serine synthesis pathway is essential in breast cancer". Nature 476 (7360): 346–350. doi:10.1038/nature10350. 
  3. ^ Shaheen, R; Rahbeeni, Z; Alhashem, A; Faqeih, E; Zhao, Q; Xiong, Y; Almoisheer, A; Al-Qattan, S. M.; Almadani, H. A.; Al-Onazi, N; Al-Baqawi, B. S.; Saleh, M. A.; Alkuraya, F. S. (2014). "Neu-Laxova Syndrome, an Inborn Error of Serine Metabolism, is Caused by Mutations in PHGDH". The American Journal of Human Genetics 94 (6): 898–904. doi:10.1016/j.ajhg.2014.04.015. PMID 24836451.  edit

Further reading[edit]