維基百科

穀胱甘肽還原酶

穀胱甘肽還原酶[1]（英語：Glutathione reductase，EC 1.8.1.7）是一種將氧化型穀胱甘肽（GSSG）還原成為硫醇型穀胱甘肽的酶，而穀胱甘肽是一種重要的細胞抗氧化劑[2][3]。

穀胱甘肽還原酶
PDB rendering based on 1GRE.
有效結構
PDB 直系同源檢索：PDBe, RCSB
標識
代號 GSR; MGC78522
擴展標識 遺傳學：138300 鼠基因：95804 同源基因：531 GeneCards: GSR Gene
EC編號 1.8.1.7
RNA表達模式
更多表達數據
直系同源體
物種 人類 小鼠
Entrez 2936 14782
Ensembl ENSG00000104687 ENSMUSG00000031584
UniProt P00390 n/a
mRNA序列 NM_000637.3 NM_010344.4
蛋白序列 NP_000628.2 NP_034474.4
基因位置 Chr 8:
30.54 – 30.59 Mb		 Chr 8:
34.76 – 34.81 Mb
PubMed查詢 [2] [3]

對於一摩爾的氧化型穀胱甘肽（GSSG），需要一摩爾的NADPH將氧化型穀胱甘肽還原為還原型穀胱甘肽。這種酶形成一個FAD結合的同型二聚體。穀胱甘肽還原酶在所有界中都是進化保守的。在細菌、酵母與動物中，編碼穀胱甘肽還原酶的基因是同一種；然而，在植物基因組中，有兩個被編碼的穀胱甘肽還原酶。果蠅與錐體蟲甚至都沒有編碼穀胱甘肽還原酶的基因[4]。在這些生物中，穀胱甘肽還原酶的還原是分別由硫氧還蛋白以及錐蟲胱甘肽系統來完成的[4][5]。

以NADPH為氫供體、氧化型穀胱甘肽為氫受體的還原酶，反應生成NADP+和還原型穀胱甘肽。

參考文獻

編輯
  1. ^ [1][永久失效連結]
  2. ^ Meister A. Glutathione metabolism and its selective modification. J. Biol. Chem. 1988, 263 (33): 17205–8 [2011-09-19]. PMID 3053703. （原始內容存檔於2009-08-17）. 
  3. ^ Mannervik B. The enzymes of glutathione metabolism: an overview. Biochem. Soc. Trans. 1987, 15 (4): 717–8. PMID 3315772. 
  4. ^ 4.0 4.1 Kanzok SM, Fechner A, Bauer H, Ulschmid JK, Müller HM, Botella-Munoz J, Schneuwly S, Schirmer R, Becker K. Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science. 2001, 291 (5504): 643–6. PMID 11158675. doi:10.1126/science.291.5504.643. 
  5. ^ Krauth-Siegel RL, Comini MA. Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism. Biochim Biophys Acta. 2008, 1780 (11): 1236–48. PMID 18395526. doi:10.1016/j.bbagen.2008.03.006. 

深入閱讀

編輯
  • Sinet PM, Bresson JL, Couturier J; et al. [Possible localization of the glutathione reductase (EC 1.6.4.2) on the 8p21 band]. Ann. Genet. 1977, 20 (1): 13–7. PMID 302667. 
  • Krohne-Ehrich G, Schirmer RH, Untucht-Grau R. Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide.. Eur. J. Biochem. 1978, 80 (1): 65–71. PMID 923580. doi:10.1111/j.1432-1033.1977.tb11856.x. 
  • Loos H, Roos D, Weening R, Houwerzijl J. Familial deficiency of glutathione reductase in human blood cells.. Blood. 1976, 48 (1): 53–62. PMID 947404. 
  • Tutic M, Lu XA, Schirmer RH, Werner D. Cloning and sequencing of mammalian glutathione reductase cDNA.. Eur. J. Biochem. 1990, 188 (3): 523–8. PMID 2185014. doi:10.1111/j.1432-1033.1990.tb15431.x. 
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  • Pai EF, Schulz GE. The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates.. J. Biol. Chem. 1983, 258 (3): 1752–7. PMID 6822532. 
  • Krauth-Siegel RL, Blatterspiel R, Saleh M; et al. Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain.. Eur. J. Biochem. 1982, 121 (2): 259–67. PMID 7060551. doi:10.1111/j.1432-1033.1982.tb05780.x. 
  • Thieme R, Pai EF, Schirmer RH, Schulz GE. Three-dimensional structure of glutathione reductase at 2 A resolution.. J. Mol. Biol. 1982, 152 (4): 763–82. PMID 7334521. doi:10.1016/0022-2836(81)90126-1. 
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  • Nordhoff A, Tziatzios C, van den Broek JA; et al. Denaturation and reactivation of dimeric human glutathione reductase--an assay for folding inhibitors. Eur. J. Biochem. 1997, 245 (2): 273–82. PMID 9151953. doi:10.1111/j.1432-1033.1997.00273.x. 
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  • Zatorska A, Józwiak Z. Involvement of glutathione and glutathione-related enzymes in the protection of normal and trisomic human fibroblasts against daunorubicin. Cell Biol. Int. 2003, 26 (5): 383–91. PMID 12095224. doi:10.1006/cbir.2002.0861. 
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