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

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

Related Research Articles

Farnesyl pyrophosphate (FPP), also known as farnesyl diphosphate (FDP), is an intermediate in the biosynthesis of terpenes and terpenoids such as sterols and carotenoids. It is also used in the synthesis of CoQ, as well as dehydrodolichol diphosphate.

<span class="mw-page-title-main">Acetolactate synthase</span> Class of enzymes

The acetolactate synthase (ALS) enzyme is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids.

<span class="mw-page-title-main">Isopentenyl-diphosphate delta isomerase</span> Class of enzymes

Isopentenyl pyrophosphate isomerase, also known as Isopentenyl-diphosphate delta isomerase, is an isomerase that catalyzes the conversion of the relatively un-reactive isopentenyl pyrophosphate (IPP) to the more-reactive electrophile dimethylallyl pyrophosphate (DMAPP). This isomerization is a key step in the biosynthesis of isoprenoids through the mevalonate pathway and the MEP pathway.

In enzymology, a di-trans,poly-cis-decaprenylcistransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a farnesyltranstransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a geranyltranstransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">GGPS1</span> Mammalian protein found in Homo sapiens

Geranylgeranyl pyrophosphate synthase is an enzyme that in humans is encoded by the GGPS1 gene.

<span class="mw-page-title-main">Polyprenyl synthetase</span>

Polyprenyl synthetases are a class of enzymes responsible for synthesis of isoprenoids. Isoprenoid compounds are synthesized by various organisms. For example, in eukaryotes the isoprenoid biosynthetic pathway is responsible for the synthesis of a variety of end products including cholesterol, dolichol, ubiquinone or coenzyme Q. In bacteria this pathway leads to the synthesis of isopentenyl tRNA, isoprenoid quinones, and sugar carrier lipids. Among the enzymes that participate in that pathway, are a number of polyprenyl synthetase enzymes which catalyze a 1'4-condensation between 5-carbon isoprene units. It has been shown that all the above enzymes share some regions of sequence similarity. Two of these regions are rich in aspartic-acid residues and could be involved in the catalytic mechanism and/or the binding of the substrates.

Geranylfarnesyl diphosphate synthase is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase . This enzyme catalyses the following chemical reaction

Geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase may refer to:

Hexaprenyl diphosphate synthase is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transferase . This enzyme catalyses the following chemical reaction

Hexaprenyl-diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase . This enzyme catalyses the following chemical reaction

All-trans-nonaprenyl-diphosphate synthase is an enzyme with systematic name geranyl-diphosphate:isopentenyl-diphosphate transtransferase . This enzyme catalyses the following chemical reaction

Ditrans,polycis-polyprenyl diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase . This enzyme catalyses the following chemical reaction

Tritrans,polycis-undecaprenyl-diphosphate synthase is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate cistransferase . This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">All-trans-octaprenyl-diphosphate synthase</span> Class of enzymes

All-trans-octaprenyl-diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase . This enzyme catalyses the following chemical reaction

All-trans-decaprenyl-diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase . This enzyme catalyses the following chemical reaction

All-trans-phytoene synthase is an enzyme with systematic name geranylgeranyl-diphosphate:geranylgeranyl-diphosphate geranylgeranyltransferase . This enzyme catalyses the following chemical reaction

(+)-α-Barbatene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -α-barbatene-forming). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Aclonifen</span> Chemical compound

Aclonifen is a diphenyl ether herbicide which has been used in agriculture since the 1980s. Its mode of action has been uncertain, with evidence suggesting it might interfere with carotenoid biosynthesis or inhibit the enzyme protoporphyrinogen oxidase (PPO). Both mechanisms could result in the observed whole-plant effect of bleaching and the compound includes chemical features that are known to result in PPO effects, as seen with acifluorfen, for example. In 2020, further research revealed that aclonifen has a different and novel mode of action, targeting solanesyl diphosphate synthase which would also cause bleaching.

References

  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.