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Geranyl pyrophosphate (GPP), also known as geranyl diphosphate (GDP), is the pyrophosphate ester of the terpenoid geraniol. Its salts are colorless. Its salts are colorless. It is a precursor to many thousands of natural products .
Geranylgeranyl pyrophosphate is an intermediate in the biosynthesis of diterpenes and diterpenoids. [1] It is also the precursor to carotenoids , gibberellins , tocopherols , and chlorophylls . It is also a precursor to geranylgeranylated proteins, which is its primary use in human cells.
Both triammonium salts evolve ammonia. In contrast to the unstable nature of the triammonium salts, the diammonium phosphate (NH 4) 2 HPO 4 and monoammonium salt (NH 4)H 2 PO 4 are stable materials that are commonly used as fertilizers to provide plants with fixed nitrogen and phosphorus. [3] Ammonium phosphate is the main ingredient in pink ...
Pyrophosphorolysis is the reverse of the polymerization reaction in which pyrophosphate reacts with the 3′-nucleosidemonophosphate (NMP or dNMP), which is removed from the oligonucleotide to release the corresponding triphosphate (dNTP from DNA, or NTP from RNA). The pyrophosphate anion has the structure P 2 O 4− 7, and is an acid anhydride ...
The structure and mechanism of farnesyl pyrophosphate synthase (FPPS), a type of geranyltranstransferase, is well characterized. FPPS is a ~30 kDa Mg 2+ dependent homodimeric enzyme that synthesizes (E, E)-farnesyl pyrophosphate in a successive manner from two equivalents of isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP).
Other names in common use include bornyl pyrophosphate synthase, bornyl pyrophosphate synthetase, (+)-bornylpyrophosphate cyclase, and geranyl-diphosphate cyclase (ambiguous). This enzyme participates in monoterpenoid biosynthesis and belongs to the family of isomerases , specifically the class of intramolecular lyases.