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Volumn 443, Issue 3, 1999, Pages 251-255
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Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability
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Author keywords
Crystal structure; Flavoprotein monooxygenase; NADPH binding; p Hydroxybenzoate hydroxylase; Sequence motif; Site directed mutagenesis
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Indexed keywords
4 HYDROXYBENZOATE 3 MONOOXYGENASE;
ENZYME VARIANT;
OXYGENASE;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
UNSPECIFIC MONOOXYGENASE;
ARGININE;
FLAVINE ADENINE NUCLEOTIDE;
NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
PHENYLALANINE;
ARTICLE;
CRYSTAL STRUCTURE;
ENZYME STABILITY;
ENZYME STRUCTURE;
MUTATION;
NONHUMAN;
PRIORITY JOURNAL;
PSEUDOMONAS FLUORESCENS;
SITE DIRECTED MUTAGENESIS;
AMINO ACID SUBSTITUTION;
BINDING SITE;
CHEMISTRY;
CRYSTALLIZATION;
ENZYMOLOGY;
GENETICS;
KINETICS;
METABOLISM;
PH;
PROTEIN CONFORMATION;
SPECTROSCOPY;
TEMPERATURE;
TIME;
X RAY CRYSTALLOGRAPHY;
4-HYDROXYBENZOATE-3-MONOOXYGENASE;
AMINO ACID SUBSTITUTION;
ARGININE;
BINDING SITES;
CRYSTALLIZATION;
CRYSTALLOGRAPHY, X-RAY;
ENZYME STABILITY;
FLAVIN-ADENINE DINUCLEOTIDE;
HYDROGEN-ION CONCENTRATION;
KINETICS;
NADP;
PHENYLALANINE;
PROTEIN CONFORMATION;
PSEUDOMONAS FLUORESCENS;
SPECTRUM ANALYSIS;
TEMPERATURE;
TIME FACTORS;
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EID: 0032588643
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(98)01726-8 Document Type: Article |
Times cited : (21)
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References (24)
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