Identification of putative residues involved in the accessibility of the substrate-binding site of lipoxygenase by site-directed mutagenesis studies

Archives of Biochemistry and Biophysics

Volumn 509, Issue 1, 2011, Pages 82-89

  Palmieri Thiers, Cynthia ^a   Alberti, Jean Christophe ^a   Canaan, Stéphane ^b   Brunini, Virginie ^a   Gambotti, Claude ^a   Tomi, Félix ^a   Oliw, Ernst H ^c   Berti, Liliane ^a   Maury, Jacques ^a  

^a UNIVERSITÉ DE CORSE   (France)

^b CNRS   (France)

^c UPPSALA UNIVERSITY   (Sweden)

Author keywords

Homology modeling; Olive lipoxygenase; Site directed mutagenesis; Substrate binding accessibility

Indexed keywords

ALANINE; AMINO ACID; ISOLEUCINE; LINOLEIC ACID; LIPOXYGENASE; LIPOXYGENASE I; PHENYLALANINE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ESCHERICHIA COLI; MUTANT; NONHUMAN; PEROXIDATION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; SOYBEAN; WILD TYPE;

ALPHA-LINOLENIC ACID; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; GENE EXPRESSION; HUMANS; LINOLEIC ACID; LIPID PEROXIDATION; LIPOXYGENASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; OLEA; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

GLYCINE MAX;

EID: 79954439998     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2011.02.008     Document Type: Article

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