Polyprenyl diphosphate synthases.

  title={Polyprenyl diphosphate synthases.},
  author={Kyozo Ogura and Tanetoshi Koyama and Hiroshi Sagami},
  journal={Sub-cellular biochemistry},
It is noteworthy that in spite of the similarity of the reactions catalyzed by these prenyltransferases, the modes of expression of catalytic function are surprisingly different, varying according to the chain length and stereochemistry of reaction products. These enzymes are summarized and classified into four groups, as shown in Figure 13. Short-chain prenyl diphosphates synthases such as FPP and GGPP synthases require no cofactor except divalent metal ions, Mg2+ or Mn2+, which are commonly… 
Structure, mechanism and function of prenyltransferases.
The structures of Ras farnesyltransferase and Rab geranylgeranyltransferase are used to elucidate the reaction mechanism of this group of enzymes, and the mechanism that controls product chain length and the reaction kinetics of IPP condensation in the cis-type and trans-type enzymes are focused on.
Characterization of a Cis-Prenyltransferase from Lilium longiflorum Anther
The studies suggest that evolutional mutations may occur in the plant cis-prenyltransferase to convert it into a shorter-chain enzyme.
Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli.
The usage of protein fusion, optimized culture conditions and codon-optimization were used to allow the overexpression and purification of functionally active human DHDDS in E. coli, and the homology of cis- PT among different species suggests that this protocol may be applied for other eukaryotic cis-PT as well, such as those involved in natural rubber synthesis.
Different reaction mechanisms for cis- and trans-prenyltransferases.
Mechanism of cis-prenyltransferase reaction probed by substrate analogues.
Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase.
It is shown that the monophosphate analogue of FPP binds UPPS with an eight times lower affinity, a result of a larger dissociation rate constant, and suggests that the upper portion of the active-site tunnel, where cis double bonds of the product reside, may be critical for determining the final product chain length.
Crystal Structures of Undecaprenyl Pyrophosphate Synthase in Complex with Magnesium, Isopentenyl Pyrophosphate, and Farnesyl Thiopyrophosphate
The results here improve the understanding of the UPPs enzyme reaction significantly and suggest other conserved residues, including His43, Ser71, Asn74, and Arg77, may serve as general acid/base and pyrophosphate carrier.
Refolding and characterization of a yeast dehydrodolichyl diphosphate synthase overexpressed in Escherichia coli.
The kinetic studies indicated that the soluble and refolded DDPPs have comparable activities (k(cat) = 2 x 10(-4) s(-1)).


Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution.
The crystal structure of avian recombinant FPS, the first three-dimensional structure for any prenyltransferase, was determined to 2.6-A resolution, and suggests that the conserved aspartate residues participate in substrate binding of catalysis.
Yeast farnesyl-diphosphate synthase: site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II.
  • L. Song, C. Poulter
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1994
Addition of an -EEF epitope to the C terminus of wild-type FPPSase resulted in a 14-fold increase of KmIPP and a 12-fold decrease of kcat, suggesting that the conserved hydrophilic C termini of the enzyme may have a role in substrate binding and catalysis.
Site-directed mutagenesis of farnesyl diphosphate synthase; effect of substitution on the three carboxyl-terminal amino acids
Three kinds of mutant enzymes showed similar catalytic activities to that of the wild-type enzyme, indicating that the basic amino acids including the conserved arginine in the C-terminal region are not essential for catalytic function.
Structural and functional roles of the cysteine residues of Bacillus stearothermophilus farnesyl diphosphate synthase.
Evidence that residues other than cysteine are involved in the conversion of this enzyme into the oxidized form is provided, indicating that neither of the cysteines is essential for catalytic function.
A novel prenyltransferase from Paracoccus denitrificans.
A new polyprenyltransferase catalysing the formation of Z-double bonds was found and partially purified from extracts of Paracoccus denitrificans, the precursor of the bacterial sugar-carrier lipid.