Cysteine 10 is critical for the activity ofOchrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site-Reference-Cited by-同舟云学术

Cysteine 10 is critical for the activity ofOchrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site

Published:2008 Issue:1 Volume:71 Page:16-23
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Allocati Nerino,Federici Luca,Masulli Michele,Favaloro Bartolo,Di Ilio Carmine

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference30 articles.

1. GLUTATHIONE TRANSFERASES

2. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily

3. Glutathione transferases: new functions

4. Purification and characterization of three forms of glutathione transferase from Proteus mirabilis

5. Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106

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