Glutamate-64, a newly identified residue of the functionally conserved electron-sharing network contributes to catalysis and structural integrity of glutathione transferases

Biochemical Journal

Volumn 402, Issue 2, 2007, Pages 339-348

  Winayanuwattikun, Pakorn ^a   Ketterman, Albert J ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

Author keywords

Active site residue; Anopheles dirus; Catalytic mechanism; Electron sharing network; Glutathione transferase; Structural integrity

Indexed keywords

ACTIVE SITE RESIDUES; ANOPHELES DIRUS; CATALYTIC MECHANISM; ELECTRON SHARING NETWORKS; GLUTATHIONE TRANSFERASE;

AMINO ACIDS; CATALYSIS; CRYSTAL STRUCTURE; ELECTRONS; IONIZATION; THERMODYNAMICS;

ENZYME KINETICS;

ARGININE; ASPARTIC ACID; CHLORIDE; FLUORIDE; GLUTAMATE 64; GLUTAMIC ACID; GLUTATHIONE; GLUTATHIONE TRANSFERASE; THIOL GROUP; UNCLASSIFIED DRUG; GLUTAMIC ACID DERIVATIVE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONJUGATION; ELECTRICITY; ELECTRON; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME DENATURATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME REACTIVATION; ENZYME STABILITY; ENZYME STRUCTURE; IN VITRO STUDY; IONIZATION; NUCLEOTIDE SEQUENCE; PKA; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTON TRANSPORT; STEADY STATE; THERMODYNAMICS; WILD TYPE; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; ENZYME ACTIVATION; GENETICS; HUMAN; HYDROGEN BOND; KINETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SPECTROFLUOROMETRY; STRUCTURAL HOMOLOGY; TEMPERATURE; VISCOSITY;

ANOPHELES DIRUS;

AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CIRCULAR DICHROISM; CONSERVED SEQUENCE; ELECTRONS; ENZYME ACTIVATION; GLUTAMATES; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HUMANS; HYDROGEN BONDING; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SPECTROMETRY, FLUORESCENCE; STRUCTURAL HOMOLOGY, PROTEIN; TEMPERATURE; THERMODYNAMICS; VISCOSITY;

EID: 33847712107     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061253     Document Type: Article

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