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Volumn 277, Issue 18, 2002, Pages 15613-15620

Desaturation and hydroxylation. Residues 148 and 324 of Arabidopsis FAD2, in addition to substrate chain length, exert a major influence in partitioning of catalytic specificity

(3) Broadwater, John A a Whittle, Edward a Shanklin, John a

a BROOKHAVEN NATIONAL LABORATORY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DESATURATION;

AMINO ACIDS; ENZYME KINETICS; FATTY ACIDS; HYDROXYLATION; SUBSTITUTION REACTIONS; YEAST;

ENZYMES;

CASTOR OIL; OLEIC ACID; OXYGENASE;

AMINO ACID SUBSTITUTION; ARABIDOPSIS; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; FATTY ACID ANALYSIS; FATTY ACID DESATURATION; HYDROXYLATION; LESQUERELLA FENDLERI; NONHUMAN; PLANT; POINT MUTATION; PRIORITY JOURNAL; REACTION ANALYSIS; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; YEAST;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARABIDOPSIS; BASE SEQUENCE; BINDING SITES; BRASSICACEAE; DNA PRIMERS; FATTY ACID DESATURASES; GAS CHROMATOGRAPHY-MASS SPECTROMETRY; KINETICS; MIXED FUNCTION OXYGENASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; POINT MUTATION; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

ARABIDOPSIS; ARABIDOPSIS THALIANA; CASTOR; LESQUERELLA; LESQUERELLA FENDLERI; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0037013191 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M200231200 Document Type: Article

Times cited : (143)

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