His-311 and Arg-559 are key residues involved in fatty acid oxygenation in pathogen-inducible oxygenase

Journal of Biological Chemistry

Volumn 283, Issue 36, 2008, Pages 24962-24971

  Koszelak Rosenblum, Mary ^a   Krol, Adam C ^a   Simmons, Danielle M ^a,b   Goulah, Christopher C ^a   Wroblewski, Liliana ^b   Malkowski, Michael G ^a,b,c  

^a UNIVERSITY AT BUFFALO   (United States)

^b UNIVERSITY AT BUFFALO   (United States)

^c NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; BIOCHEMISTRY; CARBOXYLATION; CATALYSIS; CATALYSTS; ENZYME ACTIVITY; ENZYMES; FATTY ACIDS; OXYGENATION; PROTEINS;

COMPUTATIONAL SEQUENCES; CYCLOOXYGENASE; DIOXYGENASE; EXPERIMENTAL OBSERVATIONS; HIGH AFFINITY BINDINGS; HYDROPEROXIDES; LIGAND BINDING AFFINITIES; LINOLEIC ACIDS; MOLECULAR DETERMINANTS; OXYGENASE; SECONDARY STRUCTURE PREDICTIONS;

ACIDS;

ARGININE; CYCLOOXYGENASE 1; FATTY ACID; HEMOPROTEIN; HISTONE; LINOLEIC ACID; PATHOGEN INDUCIBLE OXYGENASE; UNCLASSIFIED DRUG; CYCLOOXYGENASE 2; DIOXYGENASE; LIGAND; VEGETABLE PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; LIGAND BINDING; NONHUMAN; NUCLEOTIDE SEQUENCE; OXYGENATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; RICE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; METABOLISM; MISSENSE MUTATION; OXIDATION REDUCTION REACTION; PHYSIOLOGY; SEQUENCE HOMOLOGY;

ORYZA SATIVA;

AMINO ACID SUBSTITUTION; BINDING SITES; CATALYTIC DOMAIN; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; DIOXYGENASES; LIGANDS; LINOLEIC ACID; MODELS, MOLECULAR; MUTATION, MISSENSE; ORYZA SATIVA; OXIDATION-REDUCTION; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 54049104961     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M804358200     Document Type: Article

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