Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 10, 1997, Pages 4872-4877

  Cahoon, Edgar B ^a   Lindqvist, Ylva ^b   Schneider, Gunter ^b   Shanklin, John ^a  

^a BROOKHAVEN NATIONAL LABORATORY   (United States)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

diiron; nonheme iron; protein engineering; rational design; unsaturated fatty acid

Indexed keywords

ACYL CARRIER PROTEIN; DESATURASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; ENZYME ANALYSIS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; FATTY ACID SYNTHESIS; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; DNA PRIMERS; ESCHERICHIA COLI; KINETICS; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLANT OILS; PLANTS; POINT MUTATION; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS;

EID: 0030924302     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.10.4872     Document Type: Article

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