Analysis of the Catalytic and Binding Residues of the Diadenosine Tetraphosphate Pyrophosphohydrolase from Caenorhabditis elegans by Site-directed Mutagenesis

The contributions to substrate binding and catalysis of 13 amino acid residues of the Caenorhabditis elegans diadenosine tetraphosphate pyrophosphohydrolase (Ap 4 A hydrolase) predicted from the crystal structure of an enzyme-inhibitor complex have been investigated by site-directed mutagenesis. Six...

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Veröffentlicht in:	The Journal of biological chemistry 2003-02, Vol.278 (7), p.4435-4439
Hauptverfasser:	Abdelghany, Hend M, Bailey, Scott, Blackburn, G Michael, Rafferty, John B, McLennan, Alexander G
Format:	Artikel
Sprache:	eng
Schlagworte:	Acid Anhydride Hydrolases - chemistry Acid Anhydride Hydrolases - genetics Amino Acid Sequence Animals Binding Sites - genetics Caenorhabditis elegans - enzymology Catalytic Domain - genetics Hydrolysis Molecular Sequence Data Mutagenesis, Site-Directed Substrate Specificity
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