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{{PBB|geneid=26227}} | |||
{{enzyme | |||
| Name = phosphoglycerate dehydrogenase | |||
| EC_number = 1.1.1.95 | |||
| CAS_number = | |||
| IUBMB_EC_number = 1/1/1/95 | |||
| GO_code = | |||
| image = | |||
| width = | |||
| caption = | |||
}} | |||
In [[enzymology]], a '''D-3-phosphoglycerate dehydrogenase''' ({{EC number|1.1.1.95}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]s | |||
:3-phospho-D-glycerate + NAD<sup>+</sup> <math>\rightleftharpoons</math> 3-phosphonooxypyruvate + NADH + H<sup>+</sup> | |||
:2-hydroxyglutarate + NAD<sup>+</sup> <math>\rightleftharpoons</math> 2-oxoglutarate + NADH + H<sup>+</sup> | |||
Thus, in the first case, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[3-phospho-D-glycerate]] and [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[3-phosphonooxypyruvate]], [[nicotinamide adenine dinucleotide|NADH]], and [[hydrogen ion|H<sup>+</sup>]]; in the second case, the two substrates of this enzyme are [[2-hydroxyglutarate]] and NAD<sup>+</sup>, whereas its 3 products are [[2-oxoglutarate]], NADH, and [[hydrogen ion|H<sup>+</sup>]]. | |||
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor. | |||
In humans, this enzyme is encoded by the ''PHGDH'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PHGDH phosphoglycerate dehydrogenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26227| accessdate = }}</ref> | |||
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. --> | |||
{{PBB_Summary | |||
| section_title = | |||
| summary_text = 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<sup>+</sup>/NADH as a cofactor.<ref name="entrez" /> | |||
}} | |||
Certain breast cancers are dependent on the overexpression of PHGDH.<ref>{{cite journal|last=Possemato|first=Richard|coauthors=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.|title=Functional genomics reveal that the serine synthesis pathway is essential in breast cancer|journal=Nature|date=17 August 2011|volume=476|issue=7360|pages=346–350|doi=10.1038/nature10350}}</ref> | |||
==References== | |||
{{reflist}} | |||
==Further reading== | |||
{{refbegin | 2}} | |||
{{PBB_Further_reading | |||
| citations = | |||
*{{cite journal | author=Tsang HT, Connell JW, Brown SE, ''et al.'' |title=A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex. |journal=Genomics |volume=88 |issue= 3 |pages= 333–46 |year= 2006 |pmid= 16730941 |doi= 10.1016/j.ygeno.2006.04.003 }} | |||
*{{cite journal | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }} | |||
*{{cite journal | author=Guo D, Han J, Adam BL, ''et al.'' |title=Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress. |journal=Biochem. Biophys. Res. Commun. |volume=337 |issue= 4 |pages= 1308–18 |year= 2005 |pmid= 16236267 |doi= 10.1016/j.bbrc.2005.09.191 }} | |||
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }} | |||
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }} | |||
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }} | |||
*{{cite journal | author=Pind S, Slominski E, Mauthe J, ''et al.'' |title=V490M, a common mutation in 3-phosphoglycerate dehydrogenase deficiency, causes enzyme deficiency by decreasing the yield of mature enzyme. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7136–43 |year= 2002 |pmid= 11751922 |doi= 10.1074/jbc.M111419200 }} | |||
*{{cite journal | author=Klomp LW, de Koning TJ, Malingré HE, ''et al.'' |title=Molecular characterization of 3-phosphoglycerate dehydrogenase deficiency--a neurometabolic disorder associated with reduced L-serine biosynthesis. |journal=Am. J. Hum. Genet. |volume=67 |issue= 6 |pages= 1389–99 |year= 2001 |pmid= 11055895 |doi=10.1086/316886 | pmc=1287916 }} | |||
*{{cite journal | author=Pineda M, Vilaseca MA, Artuch R, ''et al.'' |title=3-phosphoglycerate dehydrogenase deficiency in a patient with West syndrome. |journal=Developmental medicine and child neurology |volume=42 |issue= 9 |pages= 629–33 |year= 2000 |pmid= 11034457 |doi=10.1017/S0012162200001171 }} | |||
*{{cite journal | author=Baek JY, Jun DY, Taub D, Kim YH |title=Assignment of human 3-phosphoglycerate dehydrogenase (PHGDH) to human chromosome band 1p12 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=89 |issue= 1-2 |pages= 6–7 |year= 2000 |pmid= 10894924 |doi=10.1159/000015577 }} | |||
*{{cite journal | author=Cho HM, Jun DY, Bae MA, ''et al.'' |title=Nucleotide sequence and differential expression of the human 3-phosphoglycerate dehydrogenase gene. |journal=Gene |volume=245 |issue= 1 |pages= 193–201 |year= 2000 |pmid= 10713460 |doi=10.1016/S0378-1119(00)00009-3 }} | |||
*{{cite journal | author=Jaeken J, Detheux M, Van Maldergem L, ''et al.'' |title=3-Phosphoglycerate dehydrogenase deficiency: an inborn error of serine biosynthesis. |journal=Arch. Dis. Child. |volume=74 |issue= 6 |pages= 542–5 |year= 1996 |pmid= 8758134 |doi=10.1136/adc.74.6.542 | pmc=1511571 }} | |||
}} | |||
{{refend}} | |||
{{PDB Gallery|geneid=26227}} | |||
{{gene-1-stub}} | |||
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[[Category:EC 1.1.1]] | |||
[[Category:NADH-dependent enzymes]] | |||
[[Category:Enzymes of known structure]] | |||
{{1.1.1-enzyme-stub}} | |||
Latest revision as of 22:54, 19 December 2013
Template:PBB Template:Enzyme In enzymology, a D-3-phosphoglycerate dehydrogenase (Air Transportation Experts Kull from Wingham, has many interests that include butterflies, property developers in singapore and digital photography. Is a travel freak and in recent past made buy a house in singapore journey to Paleochristian and Byzantine Monuments of Thessalonika.) is an enzyme that catalyzes the chemical reactions
- 3-phospho-D-glycerate + NAD+ 3-phosphonooxypyruvate + NADH + H+
- 2-hydroxyglutarate + NAD+ 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] Template:PBB Summary Certain breast cancers are dependent on the overexpression of PHGDH.[2]
References
43 year old Petroleum Engineer Harry from Deep River, usually spends time with hobbies and interests like renting movies, property developers in singapore new condominium and vehicle racing. Constantly enjoys going to destinations like Camino Real de Tierra Adentro.
Further reading
Template:Refbegin Template:PBB Further reading Template:Refend Template:PDB Gallery
- ↑ Template:Cite web
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