Molecular basis for the reduced catalytic activity of the naturally occurring T560m mutant of human 12/15-lipoxygenase that has been implicated in coronary artery disease

Journal of Biological Chemistry

Volumn 286, Issue 27, 2011, Pages 23920-23927

  Schurmann, Kathrin ^a   Anton, Monika ^a   Ivanov, Igor ^a   Richter, Constanze ^b   Kuhn, Hartmut ^a   Walther, Matthias ^a  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING PARTNERS; BONDING NETWORKS; CARDIO-VASCULAR DISEASE; CATALYTIC EFFICIENCIES; CORONARY ARTERY DISEASE; ENZYMATIC ACTIVITIES; HYDROGEN BOND NETWORKS; HYDROGEN BOND SYSTEMS; HYDROGEN BRIDGES; KINETIC CHARACTERIZATION; KINETIC LAG PHASE; LIPOXYGENASES; MOLECULAR BASIS; NATURALLY OCCURRING; ORTHOLOGS; SIDE-CHAINS; SINGLE NUCLEOTIDE POLYMORPHISMS; THREE-DIMENSIONAL STRUCTURE;

AMINO ACIDS; DISEASES; ENZYMES; GENES; HYDROGEN; HYDROGEN BONDS; MAMMALS;

CATALYST ACTIVITY;

ASPARAGINE; GLUTAMINE; LIPOXYGENASE; THREONINE;

ALOX15 GENE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; CORONARY ARTERY DISEASE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME STRUCTURE; HUMAN; HYDROGEN BOND; MUTANT; NONHUMAN; PRIORITY JOURNAL; SINGLE NUCLEOTIDE POLYMORPHISM;

AMINO ACID SUBSTITUTION; ANIMALS; ARACHIDONATE 12-LIPOXYGENASE; ARACHIDONATE 15-LIPOXYGENASE; CATALYSIS; CORONARY ARTERY DISEASE; HUMANS; HYDROGEN BONDING; KINETICS; MICE; MUTATION, MISSENSE; PROTEIN STRUCTURE, TERTIARY; RABBITS;

MAMMALIA; ORYCTOLAGUS CUNICULUS;

EID: 79959903255     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.211821     Document Type: Article

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