Geranylfarnesyl diphosphate synthase

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Geranylfarnesyl diphosphate synthase
Identifiers
EC no. 2.5.1.81
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Geranylfarnesyl diphosphate synthase (EC 2.5.1.81, FGPP synthase, (all-E) geranylfarnesyl diphosphate synthase, GFPS, Fgs) is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 1 isopentenyl unit). [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

geranylgeranyl diphosphate + isopentenyl diphosphate (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate

The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine.

Related Research Articles

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Geranylgeranyltransferase type 1 or simply geranylgeranyltransferase is one of the three enzymes in the prenyltransferase group. In specific terms, Geranylgeranyltransferase adds a 20-carbon isoprenoid called a geranylgeranyl group to proteins bearing a CaaX motif: a four-amino acid sequence at the carboxyl terminal of a protein. Geranylgeranyltransferase inhibitors are being investigated as anti-cancer agents.

<span class="mw-page-title-main">Rab geranylgeranyltransferase</span> Class of enzyme complexes

Rab geranylgeranyltransferase also known as (protein) geranylgeranyltransferase II is one of the three prenyltransferases. It transfers (usually) two geranylgeranyl groups to the cystein(s) at the C-terminus of Rab proteins.

<span class="mw-page-title-main">Fusicoccin</span> Chemical compound

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<span class="mw-page-title-main">Prenyltransferase</span>

Prenyltransferases (PTs) are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to isoprenyl diphosphate syntheses (IPPSs). Prenyltransferases are a functional category and include several enzyme groups that are evolutionarily independent.

Aeropyrum pernix is a species of extremophile archaea in the archaeal phylum Thermoproteota. It is an obligatorily thermophilic species. The first specimens were isolated from sediments in the sea off the coast of Japan.

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.

TRNA dimethylallyltransferase is an enzyme with systematic name dimethylallyl-diphosphate: tRNA dimethylallyltransferase. This enzyme catalyses the following chemical reaction

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

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

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

References

  1. Ogawa T, Yoshimura T, Hemmi H (February 2010). "Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: Different role, different evolution". Biochemical and Biophysical Research Communications. 393 (1): 16–20. doi:10.1016/j.bbrc.2010.01.063. PMID   20097171.
  2. Tachibana A, Yano Y, Otani S, Nomura N, Sako Y, Taniguchi M (January 2000). "Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecularevolution with alteration in product specificity". European Journal of Biochemistry. 267 (2): 321–8. doi: 10.1046/j.1432-1327.2000.00967.x . PMID   10632701.
  3. Tachibana A (March 1994). "A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis". FEBS Letters. 341 (2–3): 291–4. doi:10.1016/0014-5793(94)80475-3. PMID   8137956.
  4. Lee PC, Mijts BN, Petri R, Watts KT, Schmidt-Dannert C (November 2004). "Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution". Protein Engineering, Design & Selection. 17 (11): 771–7. doi: 10.1093/protein/gzh089 . PMID   15548566.