Increased Positive Electrostatic Potential in p-Hydroxybenzoate Hydroxylase Accelerates Hydroxylation but Slows Turnover

Biochemistry

Volumn 43, Issue 6, 2004, Pages 1569-1579

  Ortiz Maldonado, Mariliz ^a   Cole, Lindsay J ^a   Dumas, Sara M ^a   Entsch, Barrie ^a   Ballou, David P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; ELECTRIC POTENTIAL; ELECTROSTATICS; ENZYMES; ORGANIC COMPOUNDS; OXIDATION;

CONFORMATIONAL REARRANGEMENTS; MUTATION;

BIOCHEMISTRY;

4 HYDROXYBENZOATE HYDROXYLASE; FLAVIN HYDROPEROXIDE; FLAVINE ADENINE NUCLEOTIDE; HYDROPEROXIDE; OXYGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ELECTRIC POTENTIAL; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; ENZYME RELEASE; ENZYME STABILITY; GENE MUTATION; HYDROXYLATION; MOLECULAR STABILITY; NONHUMAN; OXIDATION KINETICS; OXYGENATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN STRUCTURE; REACTION ANALYSIS; REDUCTION KINETICS; STRUCTURE ANALYSIS; WILD TYPE;

4-HYDROXYBENZOATE-3-MONOOXYGENASE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; ELECTROSTATICS; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; GLUTAMINE; HYDROGEN-ION CONCENTRATION; HYDROXYLATION; OXIDATION-REDUCTION; OXYGEN; PARABENS; SUBSTRATE SPECIFICITY;

EID: 1042276703     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030193d     Document Type: Article

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