References
1. Rodrı ´guez-Concepcio ´ n M, Boronat A (2015)
Breaking new ground in the regulation of the
early steps of plant isoprenoid biosynthesis.
Curr Opin Plant Biol 25:17–22. https://doi.
org/10.1016/j.pbi.2015.04.001
2. Liang PH, Ko TP, Wang AHJ (2002) Structure, mechanism and function of prenyltransferases. Eur J Biochem 269:3339–3354.
https://doi.org/10.1046/j.1432-1033.2002.
03014.x
3. Vandermoten S, Haubruge E ´ , Cusson M
(2009) New insights into short-chain prenyltransferases: structural features, evolutionary
history and potential for selective inhibition.
Cell Mol Life Sci 66:3685–3695. https://doi.
org/10.1007/s00018-009-0100-9
4. Ambo T, Noike M, Kurokawa H, Koyama T
(2008) Cloning and functional analysis of
novel short-chain cis-prenyltransferases. Biochem Biophys Res Commun 375:536–540.
https://doi.org/10.1016/j.bbrc.2008.08.
057
5. Sallaud C, Rontein D, Onillon S, Jabes F,
Duffe P, Giacalone C, Thoraval S, Escoffier C,
Herbette G, Leonhardt N, Causse M, Tissier A
(2009) A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in
the wild tomato Solanum habrochaites. Plant
Cell 21:301–317. https://doi.org/10.1105/
tpc.107.057885
6. Schilmiller AL, Schauvinhold I, Larson M,
Xu R, Charbonneau AL, Schmidt A,
Wilkerson C, Last RL, Pichersky E (2009)
Monoterpenes in the glandular trichomes of
tomato are synthesized from a neryl diphosphate precursor rather than geranyl diphosphate. Proc Natl Acad Sci 106:10865–10870.
https://doi.org/10.1073/pnas.0904113106
7. Hsieh F-L, Chang T-H, Ko T-P, Wang AH-J
(2011) Structure and mechanism of an Arabidopsis medium/long-chain-length prenyl
pyrophosphate synthase. Plant Physiol
155:1079–1090. https://doi.org/10.1104/
pp.110.168799
8. Akhtar TA, Matsuba Y, Schauvinhold I, Yu G,
Lees HA, Klein SE, Pichersky E (2013) The
tomato cis-prenyltransferase gene family. Plant
J 73:640–652. https://doi.org/10.1111/tpj.
12063
9. Marrero PF, Poulter CD, Edwards PA (1992)
Effects of site-directed mutagenesis of the
highly conserved aspartate residues in domain
II of farnesyl diphosphate synthase activity. J
Biol Chem 267:21873–21878
10. Joly A, Edwards PA (1993) Effect of sitedirected mutagenesis of conserved aspartate
and arginine residues upon farnesyl diphosphate synthase activity. J Biol Chem
268:26983–26989
11. Tarshis LC, Yan M, Poulter CD, Sacchettini JC
(1994) Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-ANG. resolution. Biochemistry 33:10871–10877. https://
doi.org/10.1021/bi00202a004
12. Song L, Poulter CD (1994) Yeast farnesyldiphosphate synthase: site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II. Proc Natl Acad Sci U S
A 91:3044–3048
13. Koyama T, Tajima M, Sano H, Doi T, KoikeTakeshita A, Obata S, Nishino T, Ogura K
(1996) Identification of significant residues in
the substrate binding site of Bacillus stearothermophilus farnesyl diphosphate synthase. Biochemistry 35:9533–9538. https://doi.org/
10.1021/bi960137v
14. Koyama T, Gotoh Y, Nishino T (2000) Intersubunit location of the active site of farnesyl
diphosphate synthase: reconstruction of active
enzymes by hybrid-type heteromeric dimers of
site-directed
mutants.
Biochemistry
39:463–469
15. Aaron JA, Christianson DW (2010) Trinuclear
metal clusters in catalysis by terpenoid
synthases. Pure Appl Chem 82:1585–1597.
https://doi.org/10.1351/PAC-CON-09-0937
16. Ohnuma S, Hirooka K, Hemmi H, Ishida C,
Ohto C, Nishino T (1996) Conversion of
product
specificity
of
archaebacterial
geranylgeranyl-diphosphate synthase. J Biol
Chem 271:18831–18837. https://doi.org/
10.1074/jbc.271.31.18831
17. Ohnuma SI, Narita K, Nakazawa T, Ishida C,
Takeuchi Y, Ohto C, Nishino T (1996) A role
of the amino acid residue located on the fifth
position before the first aspartate-rich motif of
farnesyl diphosphate synthase on determination of the final product. J Biol Chem
271:30748–30754
18. Tarshis LC, Proteau PJ, Kellogg BA, Sacchettini JC, Poulter CD (1996) Regulation of
product chain length by isoprenyl diphosphate
synthases.
Proc
Natl
Acad
Sci
93:15018–15023. https://doi.org/10.1073/
pnas.93.26.15018
19. Wang K, Ohnuma S (1999) Chain-length
determination mechanism of isoprenyl diphosphate synthases and implications for molecular
evolution. Trends Biochem Sci 24:445–451
20. Stanley Fernandez SM, Kellogg BA, Poulter CD
(2000) Farnesyl diphosphate synthase. Altering
Determination of GGPP Synthase Activity
37
1. Rodrı ´guez-Concepcio ´ n M, Boronat A (2015)
Breaking new ground in the regulation of the
early steps of plant isoprenoid biosynthesis.
Curr Opin Plant Biol 25:17–22. https://doi.
org/10.1016/j.pbi.2015.04.001
2. Liang PH, Ko TP, Wang AHJ (2002) Structure, mechanism and function of prenyltransferases. Eur J Biochem 269:3339–3354.
https://doi.org/10.1046/j.1432-1033.2002.
03014.x
3. Vandermoten S, Haubruge E ´ , Cusson M
(2009) New insights into short-chain prenyltransferases: structural features, evolutionary
history and potential for selective inhibition.
Cell Mol Life Sci 66:3685–3695. https://doi.
org/10.1007/s00018-009-0100-9
4. Ambo T, Noike M, Kurokawa H, Koyama T
(2008) Cloning and functional analysis of
novel short-chain cis-prenyltransferases. Biochem Biophys Res Commun 375:536–540.
https://doi.org/10.1016/j.bbrc.2008.08.
057
5. Sallaud C, Rontein D, Onillon S, Jabes F,
Duffe P, Giacalone C, Thoraval S, Escoffier C,
Herbette G, Leonhardt N, Causse M, Tissier A
(2009) A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in
the wild tomato Solanum habrochaites. Plant
Cell 21:301–317. https://doi.org/10.1105/
tpc.107.057885
6. Schilmiller AL, Schauvinhold I, Larson M,
Xu R, Charbonneau AL, Schmidt A,
Wilkerson C, Last RL, Pichersky E (2009)
Monoterpenes in the glandular trichomes of
tomato are synthesized from a neryl diphosphate precursor rather than geranyl diphosphate. Proc Natl Acad Sci 106:10865–10870.
https://doi.org/10.1073/pnas.0904113106
7. Hsieh F-L, Chang T-H, Ko T-P, Wang AH-J
(2011) Structure and mechanism of an Arabidopsis medium/long-chain-length prenyl
pyrophosphate synthase. Plant Physiol
155:1079–1090. https://doi.org/10.1104/
pp.110.168799
8. Akhtar TA, Matsuba Y, Schauvinhold I, Yu G,
Lees HA, Klein SE, Pichersky E (2013) The
tomato cis-prenyltransferase gene family. Plant
J 73:640–652. https://doi.org/10.1111/tpj.
12063
9. Marrero PF, Poulter CD, Edwards PA (1992)
Effects of site-directed mutagenesis of the
highly conserved aspartate residues in domain
II of farnesyl diphosphate synthase activity. J
Biol Chem 267:21873–21878
10. Joly A, Edwards PA (1993) Effect of sitedirected mutagenesis of conserved aspartate
and arginine residues upon farnesyl diphosphate synthase activity. J Biol Chem
268:26983–26989
11. Tarshis LC, Yan M, Poulter CD, Sacchettini JC
(1994) Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-ANG. resolution. Biochemistry 33:10871–10877. https://
doi.org/10.1021/bi00202a004
12. Song L, Poulter CD (1994) Yeast farnesyldiphosphate synthase: site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II. Proc Natl Acad Sci U S
A 91:3044–3048
13. Koyama T, Tajima M, Sano H, Doi T, KoikeTakeshita A, Obata S, Nishino T, Ogura K
(1996) Identification of significant residues in
the substrate binding site of Bacillus stearothermophilus farnesyl diphosphate synthase. Biochemistry 35:9533–9538. https://doi.org/
10.1021/bi960137v
14. Koyama T, Gotoh Y, Nishino T (2000) Intersubunit location of the active site of farnesyl
diphosphate synthase: reconstruction of active
enzymes by hybrid-type heteromeric dimers of
site-directed
mutants.
Biochemistry
39:463–469
15. Aaron JA, Christianson DW (2010) Trinuclear
metal clusters in catalysis by terpenoid
synthases. Pure Appl Chem 82:1585–1597.
https://doi.org/10.1351/PAC-CON-09-0937
16. Ohnuma S, Hirooka K, Hemmi H, Ishida C,
Ohto C, Nishino T (1996) Conversion of
product
specificity
of
archaebacterial
geranylgeranyl-diphosphate synthase. J Biol
Chem 271:18831–18837. https://doi.org/
10.1074/jbc.271.31.18831
17. Ohnuma SI, Narita K, Nakazawa T, Ishida C,
Takeuchi Y, Ohto C, Nishino T (1996) A role
of the amino acid residue located on the fifth
position before the first aspartate-rich motif of
farnesyl diphosphate synthase on determination of the final product. J Biol Chem
271:30748–30754
18. Tarshis LC, Proteau PJ, Kellogg BA, Sacchettini JC, Poulter CD (1996) Regulation of
product chain length by isoprenyl diphosphate
synthases.
Proc
Natl
Acad
Sci
93:15018–15023. https://doi.org/10.1073/
pnas.93.26.15018
19. Wang K, Ohnuma S (1999) Chain-length
determination mechanism of isoprenyl diphosphate synthases and implications for molecular
evolution. Trends Biochem Sci 24:445–451
20. Stanley Fernandez SM, Kellogg BA, Poulter CD
(2000) Farnesyl diphosphate synthase. Altering
Determination of GGPP Synthase Activity
37