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Plant Physiology 75:908-913 (1984)
© 1984 American Society of Plant Biologists

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Isopentenyl Pyrophosphate cis-1,4-Polyisoprenyl Transferase from Guayule (Parthenium argentatum Gray) 1

S. Madhavan2 and Chauncey R. Benedict

Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843

Electron micrographs of the mesophyll cells of guayule Parthenium argentatum Gray leaves show deposits of cis-polyisoprene (rubber) in the cytoplasm in the vicinity of mitochondria and chloroplasts and demonstrate that the rubber-synthesizing enzymes are present in guayule leaves. The terminal step in the synthesis of cis-polyisoprene from isopentenyl pyrophosphate (IPP) catalyzed by isopentenyl pyrophosphate cis-1,4-polyisoprenyl transferase has been demonstrated in crude leaf extracts by the enzymic incorporation of [14C]isopentenyl pyrophosphate into the polymer and the recovery of [14C]levulinic acid following ozonolysis. The rubber transferase activity in the crude extracts of guayule leaves was 5.8 nanomoles isopentenyl pyrophosphate incorporated per milligram protein per hour. This is the first description of the rubber transferase from a nonlaticiferous plant.

The specific activity (in units of nanomoles IPP converted per milligram protein per hour) of the partially purified enzyme following chromatography on diethylaminoethyl-cellulose columns was 41.7 units and contained 0.29 units of IPP isomerase activity and 0.08 units of farnesyl pyrophosphate synthetase activity. The rubber transferase requires reduced glutathione and Mg2+ for maximal activity. There was no incorporation of IPP into cis-1,4-polyisoprene in the absence of rubber particles as primer, and Langmuir isotherm plots showed that the specific activity of the enzyme was proportional to the concentration of the enzyme on the surface of the rubber particles. For a given rubber particle distribution, enzyme activity was proportional to time, IPP concentration, and rubber concentration. The addition of 0.4 millimolar dimethylallyl pyrophosphate to the rubber transferase reaction resulted in a 2-fold increase in the incorporation of IPP into rubber. A comparison was made of the relative activities of rubber transferase in different species of Parthenium, Ficus, and Euphorbia.


2 Permanent address: Department of Botany, Madras Christian College, Tambaran, Madras 600059, India.

1 Funded by the Texas Agricultural Experiment Station and a research grant PCM-8104623 from the National Science Foundation.




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I. J. Kim, S. B. Ryu, Y. S. Kwak, and H. Kang
A novel cDNA from Parthenium argentatum Gray enhances the rubber biosynthetic activity in vitro*
J. Exp. Bot., February 1, 2004; 55(396): 377 - 385.
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H. Kang, M. Y. Kang, and K.-H. Han
Identification of Natural Rubber and Characterization of Rubber Biosynthetic Activity in Fig Tree
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Copyright © 1984 by the American Society of Plant Biologists