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

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Short description: Class of enzymes
All-trans-nonaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific)
Identifiers
EC number2.5.1.85
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] 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

  1. "Cloning and kinetic characterization of Arabidopsis thaliana solanesyl diphosphate synthase". The Biochemical Journal 370 (Pt 2): 679–86. March 2003. doi:10.1042/BJ20021311. PMID 12437513. 
  2. "Functional analysis of two solanesyl diphosphate synthases from Arabidopsis thaliana". Bioscience, Biotechnology, and Biochemistry 69 (3): 592–601. March 2005. doi:10.1271/bbb.69.592. PMID 15784989. 
  3. "Identification and subcellular localization of two solanesyl diphosphate synthases from Arabidopsis thaliana". Plant & Cell Physiology 45 (12): 1882–8. December 2004. doi:10.1093/pcp/pch211. PMID 15653808. 
  4. Kahlau, Sabine; Schröder, Florian; Freigang, Jörg; Laber, Bernd; Lange, Gudrun; Passon, Daniel; Kleeßen, Sabrina; Lohse, Marc et al. (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. 

External links