Molecular cloning, expression and characterization of glutathione S-transferase from Mytilus edulis. 2004

Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
College of Life Sciences, Peking University, Beijing, 100871, PR China.

The gene coding for glutathione S-transferase (GST) has been isolated from the Mytilus edulis hepatopancreas. Open reading frame analysis indicated that the M. edulis GST (meGST) gene encodes a protein of 206 amino acid residues with a calculated molecular mass of 23.68 kDa. The deduced amino acid sequence showed high sequence similarity with the sequence of the pi class GST. The meGST was expressed in Escherichia coli, and the recombinant meGST was purified by affinity chromatography and characterized. The recombinant meGST exhibited high activity towards the substrates ethacrynic acid (ECA) and 1-chloro-2,4-dinitrobenzene (CDNB). Kinetic analysis with respect to CDNB as substrate gave a K(m) of 0.68 mM and a V(max) of 0.10 mmol/min per mg protein. The recombinant meGST had a maximum activity at approximately pH 8.5, and its optimum temperature was 39 degrees C. The predicted three-dimensional structure of the meGST revealed the N-terminal domain possesses a thioredoxin fold and the six helices of the C-terminal domain make a alpha-helical bundle. These features indicate that the meGST belongs to pi class GST.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004137 Dinitrochlorobenzene A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds. 1-Chloro-2,4-Dinitrobenzene,2,4-Dinitrochlorobenzene,Benzene, 1-Chloro-2,4-Dinitro-,Chlorodinitrobenzene,DNCB,1 Chloro 2,4 Dinitrobenzene,2,4 Dinitrochlorobenzene
D004976 Ethacrynic Acid A compound that inhibits symport of sodium, potassium, and chloride primarily in the ascending limb of Henle, but also in the proximal and distal tubules. This pharmacological action results in excretion of these ions, increased urinary output, and reduction in extracellular fluid. This compound has been classified as a loop or high ceiling diuretic. Edecrin,Etacrynic Acid,Ethacrinic Acid,Ethacrynate Sodium,Ethacrynic Acid, Sodium Salt,Hydromedin,Acid, Etacrynic,Acid, Ethacrinic,Acid, Ethacrynic,Sodium, Ethacrynate
D005982 Glutathione Transferase A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite. Glutathione S-Alkyltransferase,Glutathione S-Aryltransferase,Glutathione S-Epoxidetransferase,Ligandins,S-Hydroxyalkyl Glutathione Lyase,Glutathione Organic Nitrate Ester Reductase,Glutathione S-Transferase,Glutathione S-Transferase 3,Glutathione S-Transferase A,Glutathione S-Transferase B,Glutathione S-Transferase C,Glutathione S-Transferase III,Glutathione S-Transferase P,Glutathione Transferase E,Glutathione Transferase mu,Glutathione Transferases,Heme Transfer Protein,Ligandin,Yb-Glutathione-S-Transferase,Glutathione Lyase, S-Hydroxyalkyl,Glutathione S Alkyltransferase,Glutathione S Aryltransferase,Glutathione S Epoxidetransferase,Glutathione S Transferase,Glutathione S Transferase 3,Glutathione S Transferase A,Glutathione S Transferase B,Glutathione S Transferase C,Glutathione S Transferase III,Glutathione S Transferase P,Lyase, S-Hydroxyalkyl Glutathione,P, Glutathione S-Transferase,Protein, Heme Transfer,S Hydroxyalkyl Glutathione Lyase,S-Alkyltransferase, Glutathione,S-Aryltransferase, Glutathione,S-Epoxidetransferase, Glutathione,S-Transferase 3, Glutathione,S-Transferase A, Glutathione,S-Transferase B, Glutathione,S-Transferase C, Glutathione,S-Transferase III, Glutathione,S-Transferase P, Glutathione,S-Transferase, Glutathione,Transfer Protein, Heme,Transferase E, Glutathione,Transferase mu, Glutathione,Transferase, Glutathione,Transferases, Glutathione
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA

Related Publications

Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
August 2007, Experimental parasitology,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
April 1996, Molecular and biochemical parasitology,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
January 1995, The Biochemical journal,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
February 2013, Fish & shellfish immunology,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
August 1993, Xenobiotica; the fate of foreign compounds in biological systems,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
December 2001, The Biochemical journal,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
October 2007, DNA sequence : the journal of DNA sequencing and mapping,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
January 2011, Bioorganicheskaia khimiia,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
June 2024, The protein journal,
Hai-Ling Yang, and Qing-Yin Zeng, and Er-Qiu Li, and Sheng-Geng Zhu, and Xian-Wan Zhou
May 2008, Protein expression and purification,
Copied contents to your clipboard!