Studies of the mechanism of phenol hydroxylase: Effect of mutation of proline 364 to serine

Biochemistry

Volumn 41, Issue 46, 2002, Pages 13627-13636

  Xu, Dong ^a   Enroth, Cristofer ^b   Lindqvist, Ylva ^c   Ballou, David P ^a   Massey, Vincent ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

MUTATIONS;

CATALYSIS; ENZYMES; HYDROGEN BONDS; HYDROXYLATION; MUTAGENESIS; PHENOLS; RATE CONSTANTS; SUBSTRATES;

BIOCHEMISTRY;

CARBONYL DERIVATIVE; META CRESOL; MUTANT PROTEIN; OXYGENASE; PHENOL; PHENOL HYDROXYLASE; PROLINE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RESORCINOL; SERINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROGEN BOND; HYDROXYLATION; OXIDATION; PRIORITY JOURNAL; REDUCTION; TRICHOSPORON CUTANEUM;

AMINO ACID SUBSTITUTION; CATALYSIS; CATALYTIC DOMAIN; ESCHERICHIA COLI; HYDROXYLATION; KINETICS; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADP; OXIDATION-REDUCTION; PHENOL; RESORCINOLS; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; TRICHOSPORON CUTANEUM;

EID: 0037137252     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi020446n     Document Type: Article

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