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2
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Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses.奇异变形杆菌谷胱甘肽S-转移酶B1-1参与针对氧化应激和化学应激的保护机制。
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Evolutionarily conserved structural motifs in bacterial GST (glutathione S-transferase) are involved in protein folding and stability.细菌谷胱甘肽 S-转移酶（GST）中进化保守的结构基序参与蛋白质折叠和稳定性。
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4
Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses.奇异变形杆菌谷胱甘肽S-转移酶B1-1参与针对氧化应激和化学应激的保护机制。
Biochem J. 2003 Jul 1;373(Pt 1):305-11. doi: 10.1042/BJ20030184.

本文引用的文献

1
Evaluation of the role of two conserved active-site residues in beta class glutathione S-transferases.β类谷胱甘肽S-转移酶中两个保守活性位点残基的作用评估。
Biochem J. 2000 Oct 15;351 Pt 2(Pt 2):341-6.
2
Identification, characterization, and crystal structure of the Omega class glutathione transferases.ω类谷胱甘肽转移酶的鉴定、表征及晶体结构
J Biol Chem. 2000 Aug 11;275(32):24798-806. doi: 10.1074/jbc.M001706200.
3
Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress.谷胱甘肽和谷胱甘肽依赖性酶代表了一种针对氧化应激的协调调节防御机制。
Free Radic Res. 1999 Oct;31(4):273-300. doi: 10.1080/10715769900300851.
4
Functional analysis of the evolutionarily conserved proline 53 residue in Proteus mirabilis glutathione transferase B1-1.奇异变形杆菌谷胱甘肽转移酶B1-1中进化保守的脯氨酸53残基的功能分析
FEBS Lett. 1999 Feb 26;445(2-3):347-50. doi: 10.1016/s0014-5793(99)00147-7.
5
Common structural features of MAPEG -- a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism.MAPEG的常见结构特征——一个广泛存在的膜相关蛋白超家族，在类花生酸和谷胱甘肽代谢中具有高度不同的功能。
Protein Sci. 1999 Mar;8(3):689-92. doi: 10.1110/ps.8.3.689.
6
Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106.与谷胱甘肽磺酸盐复合的大肠杆菌谷胱甘肽S-转移酶的三维结构：Cys10和His106的催化作用
J Mol Biol. 1998 Aug 7;281(1):135-47. doi: 10.1006/jmbi.1998.1927.
7
A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications.细菌谷胱甘肽转移酶中的混合二硫键：功能及进化意义
Structure. 1998 Jun 15;6(6):721-34. doi: 10.1016/s0969-2126(98)00074-4.
8
Site-directed mutagenesis of the Proteus mirabilis glutathione transferase B1-1 G-site.奇异变形杆菌谷胱甘肽转移酶B1-1 G位点的定点诱变
FEBS Lett. 1998 Feb 20;423(2):122-4. doi: 10.1016/s0014-5793(98)00080-5.
9
Structure, catalytic mechanism, and evolution of the glutathione transferases.谷胱甘肽转移酶的结构、催化机制及进化
Chem Res Toxicol. 1997 Jan;10(1):2-18. doi: 10.1021/tx960072x.
10
The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance.谷胱甘肽S-转移酶超基因家族：谷胱甘肽S-转移酶的调控及其同工酶在癌症化学保护和耐药性中的作用。
Crit Rev Biochem Mol Biol. 1995;30(6):445-600. doi: 10.3109/10409239509083491.

谷氨酸-65是奇异变形杆菌谷胱甘肽S-转移酶B1-1催化作用的必需残基。

Glutamic acid-65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1.

作者信息

Allocati Nerino, Masulli Michele, Casalone Enrico, Santucci Silvia, Favaloro Bartolo, Parker Michael W, Di Ilio Carmine

机构信息

Dipartimento di Scienze Biomediche, Università G. D'Annunzio, Via dei Vestini 31, I-66013 Chieti, Italy.

出版信息

Biochem J. 2002 Apr 1;363(Pt 1):189-93. doi: 10.1042/0264-6021:3630189.

DOI:10.1042/0264-6021:3630189
PMID:11903062
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1222466/
Abstract

The functional role of three conserved amino acid residues in Proteus mirabilis glutathione S-transferase B1-1 (PmGST B1-1) has been investigated by site-directed mutagenesis. Crystallographic analyses indicated that Glu(65), Ser(103) and Glu(104) are in hydrogen-bonding distance of the N-terminal amino group of the gamma-glutamyl moiety of the co-substrate, GSH. Glu(65) was mutated to either aspartic acid or leucine, and Ser(103) and Glu(104) were both mutated to alanine. Glu(65) mutants (Glu(65)-->Asp and Glu(65)-->Leu) lost all enzyme activity, and a drastic decrease in catalytic efficiency was observed for Ser(103)-->Ala and Glu(104)-->Ala mutants toward both 1-chloro-2,4-dinitrobenzene and GSH. On the other hand, all mutants displayed similar intrinsic fluorescence, CD spectra and thermal stability, indicating that the mutations did not affect the structural integrity of the enzyme. Taken together, these results indicate that Ser(103) and Glu(104) are significantly involved in the interaction with GSH at the active site of PmGST B1-1, whereas Glu(65) is crucial for catalysis.

摘要

通过定点诱变研究了奇异变形杆菌谷胱甘肽S-转移酶B1-1（PmGST B1-1）中三个保守氨基酸残基的功能作用。晶体学分析表明，Glu(65)、Ser(103)和Glu(104)与共底物GSH的γ-谷氨酰部分的N端氨基处于氢键距离。将Glu(65)突变为天冬氨酸或亮氨酸，将Ser(103)和Glu(104)都突变为丙氨酸。Glu(65)突变体（Glu(65)→Asp和Glu(65)→Leu）失去了所有酶活性，并且观察到Ser(103)→Ala和Glu(104)→Ala突变体对1-氯-2,4-二硝基苯和GSH的催化效率急剧下降。另一方面，所有突变体都表现出相似的内在荧光、圆二色光谱和热稳定性，表明这些突变不影响酶的结构完整性。综上所述，这些结果表明Ser(103)和Glu(104)在PmGST B1-1活性位点与GSH的相互作用中起重要作用，而Glu(65)对催化至关重要。