Polyprenyl diphosphate synthases.

@article{Ogura1997PolyprenylDS,
  title={Polyprenyl diphosphate synthases.},
  author={Kyozo Ogura and Tanetoshi Koyama and Hiroshi Sagami},
  journal={Sub-cellular biochemistry},
  year={1997},
  volume={28},
  pages={
          57-87
        }
}
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… 
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References

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TLDR
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.
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    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
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TLDR
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TLDR
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TLDR
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.
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