Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase

Journal of Biological Chemistry

Volumn 286, Issue 52, 2011, Pages 44491-44502

  Tongsook, Chanakan ^a   Sucharitakuls, Jeerus ^b   Thotsaporns, Kittisak ^b   Chaiyen, Pimchai ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

^b CHULALONGKORN UNIVERSITY   (Thailand)

Author keywords

[No Author keywords available]

Indexed keywords

ADVERSE EFFECT; CONVERSION RATIO; ELECTROPHILIC AROMATIC SUBSTITUTIONS; HYDROXYL GROUPS; KEY COMPONENT; MONOOXYGENASES; OXYGEN ATOM TRANSFER; OXYGENASES; PH RANGE; PHENOLIC GROUPS; POSITIVE CHARGES; POSITIVELY CHARGED; PRODUCT FORMATION; REACTIVE INTERMEDIATE; SELECTIVE BINDING; SUBSTRATE BINDING; TWO-COMPONENT; WILD TYPES; WILD-TYPE ENZYMES;

CATALYSIS; ENZYMES; PH; PHENOLS; RATE CONSTANTS;

HYDROXYLATION;

ENZYME VARIANT; HISTIDINE; HYDROXYL GROUP; HYDROXYPHENYLACETATE 3 HYDROXYLASE; OXYGEN; OXYGENASE; PHENOL DERIVATIVE; SERINE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CHEMICAL BINDING; CHEMICAL INTERACTION; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME STRUCTURE; HYDROXYLATION; IONIZATION; PH; PRIORITY JOURNAL; PROTON TRANSPORT; SUBSTITUTION REACTION; WILD TYPE;

ACINETOBACTER BAUMANNII; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; HYDROXYBENZOIC ACIDS; HYDROXYLATION; MIXED FUNCTION OXYGENASES; MUTATION, MISSENSE; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84455161802     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.284463     Document Type: Article

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