All-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific)

All-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific) (EC 2.5.1.84, nonaprenyl diphosphate synthase, solanesyl diphosphate synthase, SolPP synthase, SPP-synthase, SPP synthase, solanesyl-diphosphate synthase, OsSPS2) is an enzyme with systematic name geranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 7 isopentenyl units).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

All-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific)
Identifiers
EC no.2.5.1.84
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
geranyl diphosphate + 7 isopentenyl diphosphate 7 diphosphate + all-trans-nonaprenyl diphosphate

This enzyme is involved in the synthesis of the side chain of menaquinone-9.

References

edit
  1. ^ Sagami H, Ogura K, Seto S (October 1977). "Solanesyl pyrophosphate synthetase from Micrococcus lysodeikticus". Biochemistry. 16 (21): 4616–22. doi:10.1021/bi00640a014. PMID 911777.
  2. ^ Fujii H, Sagami H, Koyama T, Ogura K, Seto S, Baba T, Allen CM (October 1980). "Variable product specificity of solanesyl pyrophosphate synthetase". Biochemical and Biophysical Research Communications. 96 (4): 1648–53. doi:10.1016/0006-291X(80)91363-7. PMID 7447947.
  3. ^ Ohara K, Sasaki K, Yazaki K (June 2010). "Two solanesyl diphosphate synthases with different subcellular localizations and their respective physiological roles in Oryza sativa". Journal of Experimental Botany. 61 (10): 2683–92. doi:10.1093/jxb/erq103. PMC 2882263. PMID 20421194.
  4. ^ Ohnuma S, Koyama T, Ogura K (December 1991). "Purification of solanesyl-diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase". The Journal of Biological Chemistry. 266 (35): 23706–13. PMID 1748647.
  5. ^ Gotoh T, Koyama T, Ogura K (July 1992). "Farnesyl diphosphate synthase and solanesyl diphosphate synthase reactions of diphosphate-modified allylic analogs: the significance of the diphosphate linkage involved in the allylic substrates for prenyltransferase". Journal of Biochemistry. 112 (1): 20–7. PMID 1429508.
  6. ^ Teclebrhan H, Olsson J, Swiezewska E, Dallner G (November 1993). "Biosynthesis of the side chain of ubiquinone:trans-prenyltransferase in rat liver microsomes". The Journal of Biological Chemistry. 268 (31): 23081–6. PMID 8226825.
edit