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.
Geranylgeranyl pyrophosphate is an intermediate in the biosynthesis of diterpenes and diterpenoids. It is also the precursor to carotenoids, gibberellins, tocopherols, and chlorophylls.
In enzymology, an ent-copalyl diphosphate synthase is an enzyme that catalyzes the chemical reaction:
The enzyme aristolochene synthase catalyzes the chemical reaction
The enzyme casbene synthase catalyzes the chemical reaction
The enzyme pentalenene synthase catalyzes the chemical reaction
The enzyme trichodiene synthase catalyzes the chemical reaction
In enzymology, a di-trans,poly-cis-decaprenylcistransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a geranyltranstransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a heptaprenyl diphosphate synthase 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.
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
All-trans-nonaprenyl diphosphate synthase is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase . 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
(2Z,6Z)-farnesyl diphosphate synthase is an enzyme with systematic name dimethylallyl-diphosphate:isopentenyl-diphosphate cistransferase . This enzyme catalyses the following chemical reaction
The squalene/phytoene synthase family represents proteins that catalyze the head-to-head condensation of C15 and C20 prenyl units (i.e. farnesyl diphosphate and genranylgeranyl diphosphate). This enzymatic step constitutes part of steroid and carotenoid biosynthesis pathway. Squalene synthase EC (SQS) and Phytoene synthase EC (PSY) are two well-known examples of this protein family and share a number of functional similarities. These similarities are also reflected in their primary structure. In particular three well conserved regions are shared by SQS and PSY; they could be involved in substrate binding and/or the catalytic mechanism. SQS catalyzes the conversion of two molecules of farnesyl diphosphate (FPP) into squalene. It is the first committed step in the cholesterol biosynthetic pathway. The reaction carried out by SQS is catalyzed in two separate steps: the first is a head-to-head condensation of the two molecules of FPP to form presqualene diphosphate; this intermediate is then rearranged in a NADP-dependent reduction, to form squalene:
