A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5′-nucleotidase

Biochemistry

Volumn 44, Issue 7, 2005, Pages 2244-2252

  Schultz Heienbrok, Robert ^a   Maier, Timm ^a,c   Sträter, Norbert ^b  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

^b UNIVERSITY OF LEIPZIG   (Germany)

^c ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CROSSLINKING; ENZYME INHIBITION; ENZYMES; ESCHERICHIA COLI; OXIDATION; PROTEINS; REDUCTION;

CATALYTIC MECHANISM; CD SPECTROSCOPY; DISULFIDE BRIDGES;

ENZYME KINETICS;

5' NUCLEOTIDASE; DISULFIDE;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CROSS LINKING; ENZYME ACTIVATION; ENZYME CONFORMATION; ENZYME KINETICS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

5'-NUCLEOTIDASE; ADENOSINE DIPHOSPHATE; ADENOSINE MONOPHOSPHATE; BINDING SITES; CATALYSIS; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DINUCLEOSIDE PHOSPHATES; DISULFIDES; DITHIOTHREITOL; ESCHERICHIA COLI PROTEINS; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 14044270165     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047989c     Document Type: Article

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