A double role for a strictly conserved serine: Further insights into the dUTPase catalytic mechanism

Biochemistry

Volumn 47, Issue 30, 2008, Pages 7863-7874

  Palmén, Lorena González ^a   Becker, Kristian ^b   Bülow, Leif ^b   Kvassman, Jan Olov ^a  

^a LINNAEUS UNIVERSITY   (Sweden)

^b LUND UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPLEXATION; ESCHERICHIA COLI; HYDROGEN; HYDROGEN BONDS; MAGNESIUM PRINTING PLATES; NITROGEN; OXYGEN; PHOSPHORUS; QUANTUM CHEMISTRY; SUBSTRATES;

ACTIVE SITES; BIFUNCTIONAL; CATALYTIC MECHANISMS; NEGATIVE CHARGING;

NONMETALS;

ALPHA PHOSPHORUS; ASPARAGINE; ASPARTIC ACID; BETA PHOSPHORUS; DEAMINASE; DEOXYURIDINE TRIPHOSPHATE DERIVATIVE; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; HYDROGEN; HYDROXIDE; MAGNESIUM; NITROGEN; OXYGEN; PHOSPHORUS; PYRIMIDINE; SERINE; SERINE BETA HYDROXIDE;

AMINO ACID ANALYSIS; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; DEAMINATION; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STABILITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROGEN BOND; HYDROLYSIS; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL;

ALANINE; CATALYSIS; DIMERIZATION; ENZYME STABILITY; ESCHERICHIA COLI; GUANIDINE; HYDROGEN BONDING; HYDROLYSIS; KINETICS; MAGNESIUM; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PYROPHOSPHATASES; SERINE; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 48249113725     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800325j     Document Type: Article

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