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A more recent version of this article appeared on January 25, 2002
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M105900200v1
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Papers In Press, published online ahead of print December 3, 2001
J. Biol. Chem, 10.1074/jbc.M105900200
Submitted on June 25, 2001
Revised on October 5, 2001
Accepted on December 1, 2001

Interactions with the small subunit of geranyl diphosphate synthase modifies the chain length specificity of geranylgeranyl diphosphate synthase to produce geranyl diphosphate

Charles Burke and Rodney Croteau

Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340

Corresponding Author: croteau{at}mail.wsu.edu

Geranyl diphosphate synthase belongs to a subgroup of prenyltransferases, including farnesyl diphosphate synthase and geranylgeranyl diphosphate synthase, which catalyze the specific formation, from C5 units, of the respective C10, C15, and C20 precursors of monoterpenes, sesquiterpenes and diterpenes. Unlike farnesyl diphosphate synthase and geranylgeranyl diphosphate synthase, which are homodimers, geranyl diphosphate synthase from Mentha is a heterotetramer in which the large subunit shares functional motifs and a high level of amino acid sequence identity (56-75%) with geranylgeranyl diphosphate synthases of plant origin. The small subunit, however, shares little sequence identity with other isoprenyl diphosphate synthases; yet, it is absolutely required for geranyl diphosphate synthase catalysis. Coexpression in Escherichia coli of the Mentha geranyl diphosphate synthase small subunit with the phylogenetically distant geranylgeranyl diphosphate synthase from Taxus canadensis and Abies grandis yielded a functional hybrid-heterodimer that generated geranyl diphosphate as product in each case. These results indicate that the geranyl diphosphate synthase small subunit is capable of modifying the chain length specificity of geranylgeranyl diphosphate synthase (but not, apparently, farnesyl diphosphate synthase) to favor the production of C10 chains. Comparison of the kinetic behavior of the parent prenyltransferases with that of the hybrid enzyme revealed that the hybrid possesses characteristics of both geranyl diphosphate synthase and geranylgeranyl diphosphate synthase.


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