Mutational and kinetic evaluation of conserved His-123 in dual specificity protein-tyrosine phosphatase vaccinia H1-related phosphatase: Participation of Tyr-78 and Thr-73 residues in tuning the orientation of His-123

Journal of Biological Chemistry

Volumn 276, Issue 29, 2001, Pages 27568-27574

  Kim, Jin Hahn ^a   Shin, Deug Y ^b   Han, Moon Hi ^b   Choi, Myung Un ^a  

^a Seoul National University   (South Korea)

^b Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; HYDROGEN BONDS; MOLECULAR STRUCTURE; MUTAGENESIS;

MUTANTS;

BIOCHEMISTRY;

CYSTEINE; HISTIDINE; HISTONE; IMIDAZOLE; PROTEIN TYROSINE PHOSPHATASE; THREONINE; TYROSINE; UNCLASSIFIED DRUG; VACCINIA H1 RELATED PROTEIN PHOSPHATASE; PRIMER DNA; VACCINIA VIRUS H1 PHOSPHATASE HOMOLOG 5;

ARTICLE; CRYSTAL STRUCTURE; HYDROGEN BOND; KINETICS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; VACCINIA; CHEMISTRY; ENZYME SPECIFICITY; EVALUATION; GENETICS; METABOLISM; NUCLEOTIDE SEQUENCE; PH; PROTEIN CONFORMATION;

VACCINIA;

BASE SEQUENCE; CONSERVED SEQUENCE; DNA PRIMERS; EVALUATION STUDIES; HISTIDINE; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN-TYROSINE-PHOSPHATASE; SUBSTRATE SPECIFICITY; THREONINE; TYROSINE;

EID: 0035920138     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M010526200     Document Type: Article

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