Different roles of the diphosphate moieties of allylic and homoallylic diphosphates in prenyltransferase reaction

doi:10.1016/S0006-291X(88)80854-4

Biochemical and Biophysical Research Communications

Volume 156, Issue 1, 14 October 1988, Pages 396-402

https://doi.org/10.1016/S0006-291X(88)80854-4 Get rights and content

Summary

In contrast to the reactivity of geranyl methylenediphosphonate in the reaction catalyzed by farnesyl diphosphate synthase, that of isopentenyl methylenediphosphonate showed an optimum at a more acidic pH than that of isopentenyl diphosphate, and it was inhibited by magnesium ions under certain conditions. These facts suggest that isopentenyl diphosphate is engaged in the enzyme reaction in the form of metal-free substrate contrary to the allylic substrate, which reacts in the form of metalcomplexed substrate. Thus the diphosphate moieties of allylic and homoallylic substrates have different roles in the prenyl transferase reaction.

References (8)

MakiY. et al.
Tetrahedron Lett.
(1975)
PoulterC.D. et al.
GotohT. et al.
Chem. Lett.
(1987)
StremlerK.E. et al.
J. Am. Chem. Soc.
(1987)

There are more references available in the full text version of this article.

Cited by (7)

Characterization of aspen isoprene synthase, an enzyme responsible for leaf isoprene emission to the atmosphere
1995, Journal of Biological Chemistry
Isoprene (2-methyl-1,3-butadiene) is a volatile hydrocarbon emitted from many plant species to the atmosphere, where it plays an important role in atmospheric chemistry. An enzyme extracted from aspen (Populus tremuloides) leaves was previously found to catalyze the Mg²⁺-dependent elimination of pyrophosphate from dimethylallyl diphosphate (DMAPP) to form isoprene (Silver, G. M., and Fall, R.(1991) Plant Physiol. 97, 1588-1591). This enzyme, isoprene synthase, has now been purified 4000-fold to near homogeneity. The enzyme had a native molecular mass of 98-137 kDa and isoelectric point of 4.7 and contained 58- and 62-kDa subunits, implying that it is a heterodimer. Partial amino acid sequences of the two subunits indicated they are closely related to each other and that they do not share a strong homology with any other reported proteins. The isoprene synthase reaction was dependent on Mg²⁺ or Mn²⁺, and the reaction products were shown to be isoprene and pyrophosphate with a stoichiometry close to 1:1. The K_m for DMAPP was high at 8 mM, and the k_cat of 1.7 s⁻¹ was low, but similar to those of other allylic diphosphate-utilizing enzymes. It is argued that the isoprene synthase reaction may be much more efficient in vivo, where it is under light-dependent control. It seems probable that this unique enzyme, rather than non-enzymatic reactions, can account for the emission of hundreds of millions of metric tons of isoprene from plants to the global atmosphere each year.
Crystallization and preliminary X-ray diffraction studies of Bacillus stearothermophilus farnesyl diphosphate synthase expressed in Escherichia coli
1993, Journal of Molecular Biology
Thermostable farnesyl diphosphate synthase (EC 2.5.1.10) from Bacillus stearothermophilus, which was overexpressed in Escherichia coli, has been crystallized by the vapor-diffusion procedure. Tetragonal crystals were obtained using ammonium sulfate as a precipitant. The crystals diffracted X-rays to about 3 Å resolution. The diffraction pattern indicated that the space group is I4₁22 with unit-cell dimensions of a = b = 114 Å and c = 247 Å. It is thought that the asymmetric unit comprises two or three molecules of farnesyl diphosphate synthase.
Induction of two prenyltransferases for the accumulation of coumarin phytoalexins in elicitor-treated Ammi majus cell suspension cultures
1990, Phytochemistry
Two dimethylallyl diphosphate: umbelliferone dimethylallyltransferase (prenyltransferase) activities, catalysing the 6-prenylation and the 7-O-prenylation, respectively, of umbelliferone in the course of phytoalexin synthesis, increased in Ammi majus cell suspension cultures in response to elicitor treatment. Both enzyme activities were dependent on Mg²⁺ or Mn²⁺ with significant preference for Mg²⁺ in the 6-prenylation reaction. Whereas darkgrown cells did not contain these activities, both prenyltransferase activities were induced rapidly by the addition of elicitor reaching a first maximum after 10–14 hr and a second maximum beyond 30 hr. Other coumarin specific, elicitor-induced enzyme activities of A. majus cells, in contrast, showed only one maximum of activity within the 50 hr experimental period, while the pattern of induction of phenylalanine ammonia-lyase activity resembled that of the prenyltransferases with maxima at ca 8 hr and 20–30 hr. Preliminary data suggest that the apparent biphasic induction of these enzyme activities is due to post-translational enzyme modifications.
Role of metals in the reaction catalyzed by protein farnesyltransferase
2000, Biochemistry
Chain length distribution of the products formed in solanesyl diphosphate synthase reaction
1992, Journal of Biochemistry
COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase
1992, Journal of Biological Chemistry

View all citing articles on Scopus

View full text

Different roles of the diphosphate moieties of allylic and homoallylic diphosphates in prenyltransferase reaction

Summary

Tetrahedron Lett.

Chem. Lett.

J. Am. Chem. Soc.