Catalytically Active Monomer of Glutathione S-Transferase π and Key Residues Involved in the Electrostatic Interaction between Subunits

Catalytically Active Monomer of Glutathione S-Transferase π and Key Residues Involved in the Electrostatic Interaction between Subunits

Human glutathione transferase π (GST π) has been crystallized as a homodimer, with a subunit molecular mass of ∼23 kDa; however, in solution the average molecular mass depends on protein concentration, approaching that of monomer at

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Veröffentlicht in:The Journal of biological chemistry 2008-11, Vol.283 (47), p.32880-32888
Hauptverfasser: Huang, Yu-chu, Misquitta, Stephanie, Blond, Sylvie Y., Adams, Elizabeth, Colman, Roberta F.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Catalysis
Circular Dichroism
Dimerization
Glutathione S-Transferase pi - chemistry
Glutathione S-Transferase pi - metabolism
Humans
Hydrogen-Ion Concentration
Kinetics
Molecular Conformation
Molecular Sequence Data
Protein Binding
Protein Conformation
Protein Structure and Folding
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Static Electricity
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Beschreibung
Zusammenfassung:Human glutathione transferase π (GST π) has been crystallized as a homodimer, with a subunit molecular mass of ∼23 kDa; however, in solution the average molecular mass depends on protein concentration, approaching that of monomer at
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M805484200