Catalytic Plasticity of Fatty Acid Modification Enzymes Underlying Chemical Diversity of Plant Lipids

Author:

Broun Pierre1,Shanklin John1,Whittle Ed1,Somerville Chris1

Affiliation:

1. P. Broun and C. Somerville, Carnegie Institution of Washington, Department of Plant Biology, 260 Panama Street, Stanford, CA 94305, USA. J. Shanklin and E. Whittle, Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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