Document Detail


Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids.
MedLine Citation:
PMID:  9812895     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Higher plants exhibit extensive diversity in the composition of seed storage fatty acids. This is largely due to the presence of various combinations of double or triple bonds and hydroxyl or epoxy groups, which are synthesized by a family of structurally similar enzymes. As few as four amino acid substitutions can convert an oleate 12-desaturase to a hydroxylase and as few as six result in conversion of a hydroxylase to a desaturase. These results illustrate how catalytic plasticity of these diiron enzymes has contributed to the evolution of the chemical diversity found in higher plants.
Authors:
P Broun; J Shanklin; E Whittle; C Somerville
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Science (New York, N.Y.)     Volume:  282     ISSN:  0036-8075     ISO Abbreviation:  Science     Publication Date:  1998 Nov 
Date Detail:
Created Date:  1998-12-01     Completed Date:  1998-12-01     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0404511     Medline TA:  Science     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1315-7     Citation Subset:  IM    
Affiliation:
Carnegie Institution of Washington, Department of Plant Biology, 260 Panama Street, Stanford, CA 94305, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Substitution
Arabidopsis / enzymology,  genetics
Binding Sites
Catalysis
Fatty Acid Desaturases / chemistry,  genetics,  metabolism*
Fatty Acids / metabolism*
Fatty Acids, Unsaturated / metabolism*
Genes, Plant
Hydroxy Acids / metabolism
Hydroxylation
Linoleic Acid / metabolism
Mixed Function Oxygenases / chemistry,  genetics,  metabolism*
Mutagenesis, Site-Directed
Oleic Acid / metabolism
Oxidoreductases Acting on CH-CH Group Donors
Plants / enzymology*,  genetics
Plants, Genetically Modified
Recombinant Proteins / metabolism
Ricinoleic Acids / metabolism
Chemical
Reg. No./Substance:
0/Fatty Acids; 0/Fatty Acids, Unsaturated; 0/Hydroxy Acids; 0/Recombinant Proteins; 0/Ricinoleic Acids; 112-80-1/Oleic Acid; 141-22-0/ricinoleic acid; 2197-37-7/Linoleic Acid; 4103-20-2/lesquerolic acid; 7121-47-3/densipolic acid; EC 1.-/Mixed Function Oxygenases; EC 1.14.13.26/phosphatidylcholine 12-monooxygenase; EC 1.14.19.-/Fatty Acid Desaturases; EC 1.3.-/Oxidoreductases Acting on CH-CH Group Donors; EC 1.3.1.35/Phosphatidylcholine desaturase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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