Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of Histidine 162 and Arginine 269 variants

Journal of Biological Chemistry

Volumn 273, Issue 33, 1998, Pages 21031-21039

  Eppink, Michel H M ^a   Schreuder, Herman A ^b   Van Berkel, Willem J H ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b SANOFI   (France)

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYBENZOATE 3 MONOOXYGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION;

4-HYDROXYBENZOATE-3-MONOOXYGENASE; ARGININE; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NADP; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

EID: 0032516920     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.33.21031     Document Type: Article

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