Probing a novel potato lipoxygenase with dual positional specificity reveals primary determinants of substrate binding and requirements for a surface hydrophobic loop and has implications for the role of lipoxygenases in tubers

Biochemical Journal

Volumn 353, Issue 2, 2001, Pages 345-355

  Hughes, R K ^a   West, S I ^a   Hornostaj, A R ^a   Lawson, D M ^a   Fairhurst, S A ^a   Sanchez, R O ^a   Hough, P ^a   Robinson, B H ^a   Casey, R ^a  

^a JOHN INNES CENTRE   (United Kingdom)

Author keywords

Modelling; Mutagenesis

Indexed keywords

COMPLEMENTARY DNA; LINOLEIC ACID; LIPOXYGENASE;

ARTICLE; DNA SEQUENCE; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GENE DELETION; HYDROPHOBICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; POTATO; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

BINDING SITES; CLONING, MOLECULAR; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; LIPOXYGENASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHYLOGENY; PLANT PROTEINS; SOLANUM TUBEROSUM; SUBSTRATE SPECIFICITY;

CUCUMIS SATIVUS; ESCHERICHIA COLI; PISUM SATIVUM; SOLANUM TUBEROSUM;

EID: 0035863234     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3530345     Document Type: Article

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