Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme

FEBS Journal

Volumn 274, Issue 16, 2007, Pages 4188-4198

  Johansson, Eva ^a,b,c   Thymark, Majbritt ^b   Bynck, Julie H ^b   Fanø, Mathias ^b   Larsen, Sine ^b,c   Willemoës, Martin ^b  

^a NOVO NORDISK A S   (Denmark)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

Author keywords

Deamination; Deoxynucleotide metabolism; dUTP; Enzyme regulation; Hysteresis

Indexed keywords

DEAMINASE; DEOXYCYTIDINE TRIPHOSPHATE; HISTIDINE; VALINE;

ALLOSTERISM; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STEADY STATE; WILD TYPE;

ALGORITHMS; ALLOSTERIC REGULATION; ALLOSTERIC SITE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; ESCHERICHIA COLI PROTEINS; KINETICS; MODELS, MOLECULAR; MUTANT PROTEINS; NUCLEOTIDE DEAMINASES; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; THYMINE NUCLEOTIDES;

ESCHERICHIA COLI;

EID: 34547743104     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05945.x     Document Type: Article

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