Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the α-hydroxylation of sphingolipid-associated very long chain fatty acids

Journal of Biological Chemistry

Volumn 272, Issue 45, 1997, Pages 28281-28288

  Mitchell, Andrew G ^a   Martin, Charles E ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B5; HYBRID PROTEIN; SPHINGOLIPID; VERY LONG CHAIN FATTY ACID;

ARABIDOPSIS; ARTICLE; FATTY ACID METABOLISM; GENE DISRUPTION; GENE EXPRESSION; GENE ISOLATION; HYDROXYLATION; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; BASE SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 ENZYME SYSTEM; CYTOCHROMES B5; FATTY ACIDS; HYDROXYLATION; MIXED FUNCTION OXYGENASES; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; PLANT PROTEINS; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SEQUENCE HOMOLOGY, NUCLEIC ACID; SPHINGOLIPIDS;

EID: 0030724890     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.45.28281     Document Type: Article

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