Similarities and differences in rubber biochemistry among plant species

被引:217
作者
Cornish, K [1 ]
机构
[1] USDA ARS, Western Reg Res Ctr, Albany, CA 94710 USA
关键词
Ficus elastica; Moraceae; Hevea brasiliensis; Euphorbiaceae; Parthenium argentatum; compositae; natural rubber; rubber transferase; electron paramagnetic resonance spectroscopy;
D O I
10.1016/S0031-9422(01)00097-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This report reviews aspects of the biochemical regulation of rubber yield and rubber quality in three contrasting rubber-producing species, Hevea brasiliensis, Parthenium argentatum and Ficus elastica. Although many similarities are revealed, considerable differences also exist in enzymatic mechanisms regulating biosynthetic rate and the molecular weight of the rubber biopolymers produced. In all three species. rubber molecule initiation, biosynthetic rate and molecular weight, in vitro; are dependent upon substrate concentration and the ratio of isopentenyl pyrophosphate (IPP, the elongation substrate. or monomer) and farnesyl pyrophosphate (FPP, an initiator), but these parameters are affected by intrinsic properties of the rubber transferases as well. All three rubber transferases are capable of producing a wide range of rubber molecular weight, depending upon substrate concentration, clearly demonstrating that the transferases are not the prime determinants of product size in vivo. However. despite these commonalities, considerable differences exist between the species with respect to cosubstrate effects, binding constants, effective concentration ranges, and the role of negative cooperativity in vitro. The P. argentatum rubber transferase appears to exert more control over the molecular weight it produces than the other two species and may, therefore, provide the best prospect for the source of genes for transformation of annual crop species. The kinetic data, from the three contrasting rubber-producing species, also were used to develop a model of the rubber transferase active site in which, in addition to separate IPP and allylic-PP binding sites, there exists a hydrophobic region that interacts with the linear portion of allylic-PP initiator proximal to the pyrophosphate. Substrate affinity increases until the active site is traversed and the rubber interior of the rubber particle is reached. The kinetic data suggest that the hydrophobic region in H. brasiliensis and F. elastica is about 1.8 nm long but only 1.3 nm in P. argentatum. The estimates are supported by measurements of the rubber particle monolayer membrane using electron paramagnetic resonance spectroscopy. Published by Elsevier Science Ltd.
引用
收藏
页码:1123 / 1134
页数:12
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