Hexaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)

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Hexaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)
Identifiers
EC no. 2.5.1.83
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Hexaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (EC 2.5.1.83, HexPS, hexaprenyl pyrophosphate synthetase, hexaprenyl diphosphate synthase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 3 isopentenyl units). [1] [2] [3] This enzyme catalyses the following chemical reaction

(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate 3 diphosphate + all-trans-hexaprenyl diphosphate

The enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate as an allylic substrate.

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.

The enzyme (+)-δ-cadinene synthase catalyzes the chemical reaction

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

Dimethylallyltranstransferase (DMATT), also known as farnesylpyrophosphate synthase (FPPS) or as farnesyldiphosphate synthase (FDPS), is an enzyme that in humans is encoded by the FDPS gene and catalyzes the transformation of dimethylallylpyrophosphate (DMAPP) and isopentenyl pyrophosphate (IPP) into farnesylpyrophosphate (FPP).

The enzyme aristolochene synthase catalyzes the chemical reaction

The enzyme pentalenene synthase catalyzes the chemical reaction

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

In enzymology, a heptaprenyl diphosphate synthase is an enzyme that catalyzes the chemical reaction

<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.

Hexaprenyl diphosphate synthase is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transferase . 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

Trans,polycis-polyprenyl diphosphate synthase is an enzyme with systematic name (2Z,6E)-farnesyl-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

5-Epiaristolochene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ( -5-epiaristolochene-forming). This enzyme catalyses the following chemical reaction

(+)-Epicubenol synthase (EC 4.2.3.64, farnesyl pyrophosphate cyclase) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((+)-epicubenol-forming). This enzyme catalyses the following chemical reaction

Patchoulol synthase (EC 4.2.3.70) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (patchoulol-forming). This enzyme catalyses the following chemical reaction

Valencene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (valencene-forming). It is a terpene cyclase enzyme responsible for the biosynthesis of valencene, a sesquiterpene, using farnesyl pyrophosphate as its substrate. The first such enzyme was isolated using orange cDNA. This enzyme catalyses the following chemical reaction

References

  1. ↑ Fujii H, Koyama T, Ogura K (December 1982). "Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26. Separation of two essential components". The Journal of Biological Chemistry. 257 (24): 14610–2. doi: 10.1016/S0021-9258(18)33320-9 . PMID   7174655.
  2. ↑ Shimizu N, Koyama T, Ogura K (March 1998). "Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase". Journal of Bacteriology. 180 (6): 1578–81. doi:10.1128/JB.180.6.1578-1581.1998. PMC   107062 . PMID   9515931.
  3. ↑ Nagaki M, Kimura K, Kimura H, Maki Y, Goto E, Nishino T, Koyama T (August 2001). "Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases". Bioorganic & Medicinal Chemistry Letters. 11 (16): 2157–9. doi:10.1016/S0960-894X(01)00391-2. PMID   11514159.
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