Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase

European Journal of Biochemistry

Volumn 259, Issue 3, 1999, Pages 809-814

  Keng, Yen Fang ^a   Wu, Li ^a   Zhang, Zhong Yin ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Leaving group dependence; pH dependence; Protein tyrosine phosphatase; Site specific mutagenesis

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ANALYSIS; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS; YERSINIA;

ARSENATES; BACTERIAL PROTEINS; BINDING SITES; ENZYME INHIBITORS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN-TYROSINE-PHOSPHATASE; TRYPTOPHAN; TUNGSTEN COMPOUNDS; YERSINIA;

BACTERIA (MICROORGANISMS); FELIS CATUS; NEGIBACTERIA; YERSINIA;

EID: 0033083853     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00090.x     Document Type: Article

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