Concerted bifunctionality of the dCTP deaminase-dUTPase from Methanocaldococcus jannaschii: A structural and pre-steady state kinetic analysis

Archives of Biochemistry and Biophysics

Volumn 490, Issue 1, 2009, Pages 42-49

  Siggaard, Julie H B ^a   Johansson, Eva ^a,b   Vognsen, Tina ^c   Helt, Signe Smedegaard ^c   Harris, Pernille ^c   Larsen, Sine ^a,b   Willemoës, Martin ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^c TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

Bifunctional; dCTP deaminase; Deamination; Deoxy ribonucleotide metabolism; dUTPase; Induced fit

Indexed keywords

DEOXYCYTIDINE PHOSPHATE DEAMINASE; DEOXYCYTIDINE TRIPHOSPHATE DEAMINASE; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; MAGNESIUM ION; NUCLEOTIDE; NUCLEOTIDYLTRANSFERASE; PHOSPHATE; PYROPHOSPHATE; UNCLASSIFIED DRUG; WATER;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; METHANOCOCCUS JANNASCHII; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN INTERACTION; STEADY STATE;

BINDING SITES; KINETICS; MAGNESIUM; METHANOCOCCACEAE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTATION; NUCLEOTIDE DEAMINASES; PHOSPHATES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PYROPHOSPHATASES; SUBSTRATE SPECIFICITY;

METHANOCALDOCOCCUS JANNASCHII;

EID: 70349451560     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.08.005     Document Type: Article

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