The flexible motif V of Epstein-Barr virus deoxyuridine 5′-Triphosphate pyrophosphatase is essential for catalysis

Journal of Biological Chemistry

Volumn 284, Issue 37, 2009, Pages 25280-25289

  Freeman, Lucy ^a   Buisson, Marlyse ^a,b   Tarbouriech, Nicolas ^a   Van der Heyden, Angéline ^a   Labbé, Pierre ^a   Burmeister, Wim P ^a,c  

^a UNIV GRENOBLE ALPES   (France)

^b HÔPITAL MICHALLON   (France)

^c INSTITUT UNIVERSITAIRE DE FRANCE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; COVALENT BONDS; SULFUR COMPOUNDS; VIRUSES;

ASPARTIC ACID RESIDUES; DEGREE OF SIMILARITY; DISULFIDE BRIDGE; ENZYMATIC ACTIVITIES; EPSTEIN-BARR VIRUS; PYROPHOSPHATASES; SEQUENCE ALIGNMENTS; SUBSTRATE BINDING;

ENZYMES;

DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; MAGNESIUM ION;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTALLIZATION; DELETION MUTANT; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; EPSTEIN BARR VIRUS; GENE DELETION; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN MOTIF;

HUMAN HERPESVIRUS 4;

EID: 70049089339     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.019315     Document Type: Article

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