Geranylfarnesyl diphosphate synthase

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
Geranylfarnesyl diphosphate synthase
Identifiers
EC no.2.5.1.81
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

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.
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