Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase

Protein Science

Volumn 16, Issue 7, 2007, Pages 1368-1378

  Puhl, Aaron A ^a   Gruninger, Robert J ^a   Greiner, Ralf ^b   Janzen, Timothy W ^a   Mosimann, Steven C ^a   Selinger, L Brent ^a  

^a UNIVERSITY OF LETHBRIDGE   (Canada)

^b FEDERAL RESEARCH INSTITUTE OF NUTRITION AND FOOD   (Germany)

Author keywords

Hydrolysis pathway; Inositol polyphosphate phosphatase; myo inositol; P loop; Phosphoinositide phosphatase; Phytase; Protein tyrosine phosphatase

Indexed keywords

BACTERIAL PROTEIN; INOSITOL POLYPHOSPHATE; PHOSPHATIDYLINOSITIDE; PHOSPHOTYROSINE;

ARTICLE; BINDING SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; KINETICS; MOLECULAR DOCKING; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DEPHOSPHORYLATION; PROTEIN HYDROLYSIS; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SELENOMONAS RUMINANTIUM; SITE DIRECTED MUTAGENESIS;

ACID ANHYDRIDE HYDROLASES; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; INOSITOL; INOSITOL PHOSPHATES; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PHYTIC ACID; PROTEIN-TYROSINE-PHOSPHATASE; SELENOMONAS; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); SELENOMONAS RUMINANTIUM;

EID: 34250815835     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062738307     Document Type: Article

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