Mechanism of phosphoryl transfer by nucleoside diphosphate kinase: pH dependence and role of the active site Lys16 and Tyr56 residues

European Journal of Biochemistry

Volumn 268, Issue 7, 2001, Pages 1964-1971

  Schneider, Benoit ^a   Babolat, Manuel ^a   Xu, Ying Wu ^b,c   Janin, Joël ^b   Véron, Michel ^a   Deville Bonne, Dominique ^a  

^a INSTITUT PASTEUR   (France)

^b LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^c Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

Dideoxynucleotides; Phosphoryl transfer; Substrate assisted catalysis; Tyrosyl titration

Indexed keywords

ASPARAGINE; LYSINE; NUCLEOSIDE DIPHOSPHATE KINASE; NUCLEOSIDE DIPHOSPHATE KINASE K16A; NUCLEOSIDE DIPHOSPHATE KINASE K16R; NUCLEOSIDE DIPHOSPHATE KINASE Y56A; NUCLEOTIDE DERIVATIVE; RIBOSE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; IONIZATION; KINETICS; PH; POINT MUTATION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; SPECTROPHOTOMETRY; TITRIMETRY;

ADENOSINE TRIPHOSPHATE; ANIMALS; ASPARAGINE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DICTYOSTELIUM; HYDROGEN-ION CONCENTRATION; KINETICS; LYSINE; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NUCLEOSIDE-DIPHOSPHATE KINASE; PHOSPHORUS; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE;

EID: 0034849175     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02070.x     Document Type: Article

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