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All-trans-nonaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific)

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All-trans-nonaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific)
Identifiers
EC no.2.5.1.85
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All-trans-nonaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific) (EC 2.5.1.85, nonaprenyl diphosphate synthase, solanesyl diphosphate synthase, At-SPS2, At-SPS1, SPS1, SPS2) is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 5 isopentenyl units).[1][2][3] This enzyme catalyses the following chemical reaction

geranylgeranyl diphosphate + 5 isopentenyl diphosphate 5 diphosphate + all-trans-nonaprenyl diphosphate

Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate.

In 2020, aclonifen was shown to inhibit the enzyme and is the first compound to have this mechanism of action as a herbicide.[4]

References

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  1. ^ Hirooka K, Bamba T, Fukusaki E, Kobayashi A (March 2003). "Cloning and kinetic characterization of Arabidopsis thaliana solanesyl diphosphate synthase". The Biochemical Journal. 370 (Pt 2): 679–86. doi:10.1042/BJ20021311. PMC 1223189. PMID 12437513.
  2. ^ Hirooka K, Izumi Y, An CI, Nakazawa Y, Fukusaki E, Kobayashi A (March 2005). "Functional analysis of two solanesyl diphosphate synthases from Arabidopsis thaliana". Bioscience, Biotechnology, and Biochemistry. 69 (3): 592–601. doi:10.1271/bbb.69.592. PMID 15784989.
  3. ^ Jun L, Saiki R, Tatsumi K, Nakagawa T, Kawamukai M (December 2004). "Identification and subcellular localization of two solanesyl diphosphate synthases from Arabidopsis thaliana". Plant & Cell Physiology. 45 (12): 1882–8. doi:10.1093/pcp/pch211. PMID 15653808.
  4. ^ Kahlau, Sabine; Schröder, Florian; Freigang, Jörg; Laber, Bernd; Lange, Gudrun; Passon, Daniel; Kleeßen, Sabrina; Lohse, Marc; Schulz, Arno; von Koskull‐Döring, Pascal; Klie, Sebastian; Gille, Sascha (October 2020). "Aclonifen targets solanesyl diphosphate synthase, representing a novel mode of action for herbicides". Pest Management Science. 76 (10): 3377–3388. doi:10.1002/ps.5781.
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