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

geranyl diphosphate + 7 isopentenyl diphosphate 7 diphosphate + all-trans-nonaprenyl diphosphate
All-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific)
Identifiers
EC number2.5.1.84
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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

References
  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.
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