The N-terminal β-barrel domain of mammalian lipoxygenases including mouse 5-lipoxygenase is not essential for catalytic activity and membrane binding but exhibits regulatory functions

Archives of Biochemistry and Biophysics

Volumn 516, Issue 1, 2011, Pages 1-9

  Walther, Matthias ^a   Hofheinz, Katharina ^a   Vogel, Robert ^a   Roffeis, Jana ^a   Kühn, Hartmut ^a  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

Eicosanoids; Lipid peroxidation; Molecular enzymology; Reaction specificity; Site directed mutagenesis; Structural biology

Indexed keywords

AMINO ACID; ARACHIDONATE 5 LIPOXYGENASE; ISOENZYME; LIPOXYGENASE; RECOMBINANT ENZYME;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; GENE; HUMAN; MAMMAL; MEMBRANE BINDING; MOUSE; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; ARACHIDONATE 12-LIPOXYGENASE; ARACHIDONATE 15-LIPOXYGENASE; ARACHIDONATE 5-LIPOXYGENASE; ESCHERICHIA COLI; GENE EXPRESSION; HUMANS; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

MAMMALIA;

EID: 81355160490     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2011.09.004     Document Type: Article

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