谷胱甘肽还原酶

谷胱甘肽还原酶
谷胱甘肽还原酶
	PDB rendering based on 1GRE.
有效结构
PDB	直系同源检索：PDBe, RCSB
PDB查询代码列表
	1ALG, 1BWC, 1DNC, 1GRA, 1GRB, 1GRE, 1GRF, 1GRG, 1GRT, 1GSN, 1K4Q, 1XAN, 2AAQ, 2GH5, 2GRT, 3DJG, 3DJJ, 3DK4, 3DK8, 3DK9, 3GRS, 3GRT, 4GR1, 4GRT, 5GRT
标识
代号	GSR; MGC78522
扩展标识	遗传学：138300 鼠基因：95804 同源基因：531 GeneCards: GSR Gene
EC编号	1.8.1.7
基因本体论描述
分子功能	· glutathione-disulfide reductase activity; · electron carrier activity; · oxidoreductase activity; · protein homodimerization activity; · glutathione binding; · flavin adenine dinucleotide binding; · NADP binding;
细胞成分	· soluble fraction; · cytoplasm; · mitochondrion; · cytosol; · external side of plasma membrane;
生物过程	· glutathione metabolic process; · spermatogenesis; · nucleobase, nucleoside and nucleotide interconversion; · cell redox homeostasis; · nucleobase, nucleoside and nucleotide metabolic process;
	Sources: Amigo / QuickGO
RNA表达模式
	更多表达数据
直系同源体
物种	人类
Entrez	2936
Ensembl	ENSG00000104687
UniProt	P00390
mRNA序列	NM_000637.3
蛋白序列	NP_000628.2
基因位置	Chr 8:; 30.54 – 30.59 Mb
PubMed查询	[2]
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谷胱甘肽还原酶^[1]（英语：Glutathione reductase，EC 1.8.1.7）是一种将氧化型谷胱甘肽（GSSG）还原成为硫醇型谷胱甘肽的酶，而谷胱甘肽是一种重要的细胞抗氧化剂^[2]^[3]。

Quick Facts 谷胱甘肽还原酶, 有效结构 ...

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对于一摩尔的氧化型谷胱甘肽（GSSG），需要一摩尔的NADPH将氧化型谷胱甘肽还原为还原型谷胱甘肽。这种酶形成一个FAD结合的同型二聚体。谷胱甘肽还原酶在所有界中都是进化保守的。在细菌、酵母与动物中，编码谷胱甘肽还原酶的基因是同一种；然而，在植物基因组中，有两个被编码的谷胱甘肽还原酶。果蝇与锥体虫甚至都没有编码谷胱甘肽还原酶的基因^[4]。在这些生物中，谷胱甘肽还原酶的还原是分别由硫氧还蛋白以及锥虫胱甘肽系统来完成的^[4]^[5]。

以NADPH为氢供体、氧化型谷胱甘肽为氢受体的还原酶，反应生成NADP⁺和还原型谷胱甘肽。

参考文献

[1]
[1]^{[永久失效链接]}
[2]
Meister A. Glutathione metabolism and its selective modification. J. Biol. Chem. 1988, 263 (33): 17205–8 [2011-09-19]. PMID 3053703. （原始内容存档于2009-08-17）.
[3]
Mannervik B. The enzymes of glutathione metabolism: an overview. Biochem. Soc. Trans. 1987, 15 (4): 717–8. PMID 3315772.
[4]
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.

深入阅读

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Stoll VS, Simpson SJ, Krauth-Siegel RL; et al. Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997, 36 (21): 6437–47. PMID 9174360. doi:10.1021/bi963074p.
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[1] [1]
[1]^{[永久失效链接]}

[pmid3053703-2] [2]
Meister A. Glutathione metabolism and its selective modification. J. Biol. Chem. 1988, 263 (33): 17205–8 [2011-09-19]. PMID 3053703. （原始内容存档于2009-08-17）.

[pmid3315772-3] [3]
Mannervik B. The enzymes of glutathione metabolism: an overview. Biochem. Soc. Trans. 1987, 15 (4): 717–8. PMID 3315772.

[Kanzok_2001-4] [4]
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.

[Krauth-Siegel_2008-5] [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.

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