Contribution of the two domains of E. coli 5′-nucleotidase to substrate specificity and catalysis

FEBS Letters

Volumn 587, Issue 5, 2013, Pages 460-466

  Krug, Ulrike ^a   Patzschke, Rica ^b   Zebisch, Matthias ^a,c   Balbach, Jochen ^b   Sträter, Norbert ^a  

^a UNIVERSITY OF LEIPZIG   (Germany)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Domain rotation; Enzyme kinetics; NMR; Phosphatase; Protein domain; Protein evolution

Indexed keywords

4 NITROPHENYL PHOSPHATE; 5' NUCLEOTIDASE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION;

5'-NUCLEOTIDASE; ADENOSINE DIPHOSPHATE; ADENOSINE MONOPHOSPHATE; ADENOSINE TRIPHOSPHATE; CATALYTIC DOMAIN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROLYSIS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 84874188877     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.01.010     Document Type: Article

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