Role of highly conserved residues in the reaction catalyzed by recombinant Δ7-sterol-c5(6)-desaturase studied by site-directed mutagenesis

Biochemistry

Volumn 39, Issue 4, 2000, Pages 701-711

  Taton, Maryse ^a   Husselstein, Tania ^a   Benveniste, Pierre ^a   Rahier, Alain ^a  

^a INST DE BIOL MOLEC DES PLANTES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

DESATURASE; GLUTAMIC ACID; HISTIDINE; LEUCINE; MUTANT PROTEIN; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; FATTY ACID DESATURATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYTOCHEMISTRY; PRIORITY JOURNAL; PROTEIN EXPRESSION; REACTION ANALYSIS; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STEROID HYDROXYLATION; STEROL METABOLISM; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ARABIDOPSIS; CATALYSIS; CONSERVED SEQUENCE; GENES, PLANT; GENETIC VECTORS; GLYCINE; HISTIDINE; HUMANS; LYSINE; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROLINE; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; THREONINE;

ARABIDOPSIS THALIANA;

EID: 0034142185     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991467t     Document Type: Article

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