Partial purification and characterization of the short-chain 
prenyltransferases, geranyl diphosphate synthase and farnesyl diphosphate 
synthase, from Abies grandis (grand fir)

Tholl, D.; Croteau, R.; Gershenzon, J.

doi:10.1006/abbi.2000.2212

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Partial purification and characterization of the short-chain prenyltransferases, geranyl diphosphate synthase and farnesyl diphosphate synthase, from Abies grandis (grand fir)

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Tholl, D.
Department of Biochemistry, MPI for Chemical Ecology, Max Planck Society;

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Gershenzon, J.
Department of Biochemistry, MPI for Chemical Ecology, Max Planck Society;

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Citation

Tholl, D., Croteau, R., & Gershenzon, J. (2001). Partial purification and characterization of the short-chain prenyltransferases, geranyl diphosphate synthase and farnesyl diphosphate synthase, from Abies grandis (grand fir). Archives of Biochemistry and Biophysics, 386(2), 233-242. doi:10.1006/abbi.2000.2212.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-A7C3-A

Abstract

In the conifer Abies grandis (grand fir), a secreted oleoresin rich in mono-, sesqui-, and diterpenes serves as a constitutive and induced defense against insects and pathogenic fungi. Geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) synthase, t