All-trans-nonaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific) | |||||||||
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Identifiers | |||||||||
EC no. | 2.5.1.85 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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 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]
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.
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.
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
Geranylgeranyl pyrophosphate synthase is an enzyme that in humans is encoded by the GGPS1 gene.
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
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
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.