Hexaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific)

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Hexaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific)
Identifiers
EC no. 2.5.1.82
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Hexaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific) (EC 2.5.1.82, HexPS, (all-E) hexaprenyl diphosphate synthase, (all-trans) hexaprenyl diphosphate synthase, hexaprenyl pyrophosphate synthase, HexPPs, hexaprenyl diphosphate synthase) is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transferase (adding 2 isopentenyl units). [1] [2] [3] This enzyme catalyses the following chemical reaction

geranylgeranyl diphosphate + 2 isopentenyl diphosphate 2 diphosphate + all-trans-hexaprenyl diphosphate

The enzyme prefers geranylgeranyl diphosphate to farnesyl 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.

Geranylgeranyl pyrophosphate is an intermediate in the biosynthesis of diterpenes and diterpenoids. It is also the precursor to carotenoids, gibberellins, tocopherols, and chlorophylls.

CRT is the gene cluster responsible for the biosynthesis of carotenoids. Those genes are found in eubacteria, in algae and are cryptic in Streptomyces griseus.

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

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

Trans,polycis-decaprenyl diphosphate synthase is an enzyme with systematic name (2Z,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesylcistransferase . 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

4,4'-diapophytoene synthase is an enzyme with systematic name farnesyl-diphosphate:farnesyl-diphosphate farnesyltransferase . This enzyme catalyses the following chemical reaction

CDP-archaeol synthase is an enzyme with systematic name CTP:2,3-bis-O-(geranylgeranyl)-sn-glycero-1-phosphate cytidylyltransferase. This enzyme catalyses the following chemical reaction

Terpentedienyl-diphosphate synthase is an enzyme with systematic name terpentedienyl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction

Saccharolobus solfataricus is a species of thermophilic archaeon. It was transferred from the genus Sulfolobus to the new genus Saccharolobus with the description of Saccharolobus caldissimus in 2018.

References

  1. Hemmi H, Ikejiri S, Yamashita S, Nishino T (February 2002). "Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus". Journal of Bacteriology. 184 (3): 615–20. doi:10.1128/JB.184.3.615-620.2002. PMC   139513 . PMID   11790729.
  2. Hemmi H, Noike M, Nakayama T, Nishino T (October 2002). "Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations". Biochemical and Biophysical Research Communications. 297 (5): 1096–101. doi:10.1016/S0006-291X(02)02348-3. PMID   12372398.
  3. Sun HY, Ko TP, Kuo CJ, Guo RT, Chou CC, Liang PH, Wang AH (December 2005). "Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures". Journal of Bacteriology. 187 (23): 8137–48. doi:10.1128/JB.187.23.8137-8148.2005. PMC   1291270 . PMID   16291686.