Mutation of cysteine 214 in Gi1 α subunit abolishes its endogenous GTPase activity

Biochemical Journal

Volumn 379, Issue 3, 2004, Pages 673-679

  Wang, Yuren ^a   Tawa, Gregory ^a   Smith, Deborah ^a   Krishnamurthy, Girija ^b   Young, Kathleen H ^a  

^a PFIZER INC   (United States)

^b WYETH RESEARCH   (United States)

Author keywords

Cysteine; G protein; GTP hydrolysis; GTPase; Site directed mutagenesis

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CATALYSIS; PHOSPHATES; SUBSTITUTION REACTIONS; TOXIC MATERIALS;

MUTATION; PROTEOLYSIS;

ENZYMES;

ALANINE; CYSTEINE; GUANINE NUCLEOTIDE; GUANOSINE TRIPHOSPHATASE; PROTEIN SUBUNIT; TRYPTOPHAN;

ALPHA CHAIN; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CHO CELL; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME BINDING; ENZYME INHIBITION; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ADENOSINE DIPHOSPHATE; ADENYLATE CYCLASE; ALANINE; AMINO ACID SUBSTITUTION; ANIMALS; CHO CELLS; CRICETINAE; CYCLIC AMP; CYSTEINE; FORSKOLIN; GTP-BINDING PROTEIN ALPHA SUBUNITS, GI-GO; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; KINETICS; MUTATION; PERTUSSIS TOXIN; PROTEIN BINDING; PROTEIN SUBUNITS; RGS PROTEINS; THERMODYNAMICS; TRYPSIN; TRYPTOPHAN;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS;

EID: 2542573213     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031343     Document Type: Article

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