磷酸甘油酸脱氢酶
位於1號人類染色體的基因
磷酸甘油酸脱氢酶（英語：phosphoglycerate dehydrogenase，EC 1.1.1.95 （页面存档备份，存于互联网档案馆）），是一种以NAD+或NADP+为受体、作用于供体CH-OH基团上的氧化还原酶。这种酶能催化以下两种酶促反应：
| 磷酸甘油酸脱氢酶 | |||||||||
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| 识别码 | |||||||||
| EC編號 | 1.1.1.95 | ||||||||
| CAS号 | 9075-29-0 | ||||||||
| 数据库 | |||||||||
| IntEnz | IntEnz浏览 | ||||||||
| BRENDA | BRENDA入口 | ||||||||
| ExPASy | NiceZyme浏览 | ||||||||
| KEGG | KEGG入口 | ||||||||
| MetaCyc | 代谢路径 | ||||||||
| PRIAM | 概述 | ||||||||
| PDB | RCSB PDB PDBj PDBe PDBsum | ||||||||
| 基因本体 | AmiGO / EGO | ||||||||
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- 3-磷酸化-D-甘油酸 + NAD+ 3-磷酸羟基丙酮酸 + NADH + H+
- 2-羟基戊二酸 + NAD+ α-酮戊二酸 + NADH + H+
在大肠杆菌（Escherichia coli）中，磷酸甘油酸脱氢酶参与催化丝氨酸生物合成的磷酸丝氨酸途径中的第一步，[1]上述可逆反应主要逆向进行。磷酸甘油酸脱氢酶可被丝氨酸或甘氨酸抑制。这种酶很不寻常，因为它还能像D-2-羟基戊二酸脱氢酶和L-2-羟基戊二酸脱氢酶一样还原α-酮戊二酸，其中，D型底物更适合磷酸甘油酸脱氢酶。[2]
参考文献 编辑
- ^ Pizer, L.I. The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase. J. Biol. Chem. 1986, 243: 2081–2089. PMID 4384871.
- ^ Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 1996, 178: 232–239. PMID 8550422.
- Sugimoto, E. and Pizer, L.I. The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase. J. Biol. Chem. 1968, 243: 2081–1089. PMID 4384871.
- Schuller, D.J., Grant, G.A. and Banaszak, L.J. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat. Struct. Biol. 1995, 2: 69–76. PMID 7719856.
扩展阅读 编辑
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- Guo D, Han J, Adam BL; et al. Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress.. Biochem. Biophys. Res. Commun. 2005, 337 (4): 1308–18. PMID 16236267. doi:10.1016/j.bbrc.2005.09.191.
- Gerhard DS, Wagner L, Feingold EA; et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).. Genome Res. 2004, 14 (10B): 2121–2127. PMC 528928
. PMID 15489334. doi:10.1101/gr.2596504. - Ota T, Suzuki Y, Nishikawa T; et al. Complete sequencing and characterization of 21,243 full-length human cDNAs.. Nat. Genet. 2004, 36 (1): 40–45. PMID 14702039. doi:10.1038/ng1285.
- Strausberg RL, Feingold EA, Grouse LH; et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.. Proc. Natl. Acad. Sci. U.S.A. 2003, 99 (26): 16899–16903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
- Pind S, Slominski E, Mauthe J; et al. V490M, a common mutation in 3-phosphoglycerate dehydrogenase deficiency, causes enzyme deficiency by decreasing the yield of mature enzyme.. J. Biol. Chem. 2002, 277 (9): 7136–7143. PMID 11751922. doi:10.1074/jbc.M111419200.
- Klomp LW, de Koning TJ, Malingré HE; et al. Molecular characterization of 3-phosphoglycerate dehydrogenase deficiency--a neurometabolic disorder associated with reduced L-serine biosynthesis.. Am. J. Hum. Genet. 2001, 67 (6): 1389–1399. PMC 1287916 . PMID 11055895. doi:10.1086/316886.
- Pineda M, Vilaseca MA, Artuch R; et al. 3-phosphoglycerate dehydrogenase deficiency in a patient with West syndrome.. Developmental medicine and child neurology. 2000, 42 (9): 629–633. PMID 11034457. doi:10.1017/S0012162200001171.
- Baek JY, Jun DY, Taub D, Kim YH. Assignment of human 3-phosphoglycerate dehydrogenase (PHGDH) to human chromosome band 1p12 by fluorescence in situ hybridization.. Cytogenet. Cell Genet. 2000, 89 (1-2): 6–7. PMID 10894924. doi:10.1159/000015577.
- Cho HM, Jun DY, Bae MA; et al. Nucleotide sequence and differential expression of the human 3-phosphoglycerate dehydrogenase gene.. Gene. 2000, 245 (1): 193–201. PMID 10713460. doi:10.1016/S0378-1119(00)00009-3.
- Jaeken J, Detheux M, Van Maldergem L; et al. 3-Phosphoglycerate dehydrogenase deficiency: an inborn error of serine biosynthesis.. Arch. Dis. Child. 1996, 74 (6): 542–545. PMC 1511571 . PMID 8758134. doi:10.1136/adc.74.6.542.
