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

All-trans-nonaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific)
Ec Number:2.5.1.85

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

\rightleftharpoons

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]

Notes and References

  1. Hirooka K, Bamba T, Fukusaki E, Kobayashi A . Cloning and kinetic characterization of Arabidopsis thaliana solanesyl diphosphate synthase . The Biochemical Journal . 370 . Pt 2 . 679–86 . March 2003 . 12437513 . 1223189 . 10.1042/BJ20021311 .
  2. Hirooka K, Izumi Y, An CI, Nakazawa Y, Fukusaki E, Kobayashi A . Functional analysis of two solanesyl diphosphate synthases from Arabidopsis thaliana . Bioscience, Biotechnology, and Biochemistry . 69 . 3 . 592–601 . March 2005 . 15784989 . 10.1271/bbb.69.592 . free .
  3. Jun L, Saiki R, Tatsumi K, Nakagawa T, Kawamukai M . Identification and subcellular localization of two solanesyl diphosphate synthases from Arabidopsis thaliana . Plant & Cell Physiology . 45 . 12 . 1882–8 . December 2004 . 15653808 . 10.1093/pcp/pch211 . free .
  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 . Aclonifen targets solanesyl diphosphate synthase, representing a novel mode of action for herbicides . Pest Management Science . October 2020 . 76 . 10 . 3377–3388 . 10.1002/ps.5781.