Differences in the subunit interface residues of alternatively spliced glutathione transferases affects catalytic and structural functions

Biochemical Journal

Volumn 401, Issue 3, 2007, Pages 635-644

  Piromjitpong, Juthamart ^a   Wongsantichon, Jantana ^a   Ketterman, Albert J ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

Author keywords

Anopheles dirus; Glutathione transferase (GST); Hydrophobic interaction; Subunit interface

Indexed keywords

AMINO ACIDS; BACTERIA; CATALYSIS; ELECTROSTATICS; ENZYME KINETICS; HYDROPHOBICITY; IONS; MOLECULAR STRUCTURE;

ANOPHELES DIRUS; GLUTATHIONE TRANSFERASE (GST); HYDROPHOBIC INTERACTIONS; SUBUNIT INTERFACES;

ENZYMES;

AMINO ACID DERIVATIVE; DIMER; GLUTATHIONE TRANSFERASE; ISOENZYME;

ALTERNATIVE RNA SPLICING; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; DIMERIZATION; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; HYDROPHOBICITY; MOLECULAR INTERACTION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS; STEADY STATE;

ALTERNATIVE SPLICING; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATALYSIS; GLUTATHIONE TRANSFERASE; INSECTS; MOLECULAR SEQUENCE DATA; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS;

ANOPHELES DIRUS; HEXAPODA; MAMMALIA;

EID: 33846862217     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060603     Document Type: Article

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