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Terpene synthase C terminal domain

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Terpene_synth_C
5-epi-aristolochene synthase from nicotiana tabacum
Identifiers
SymbolTerpene_synth_C
PfamPF03936
InterProIPR005630
SCOP25eau / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the C terminal domain of the TPS protein.

Function

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Terpenes synthases have a role in producing important molecules in metabolism, these molecules are part of a large group called terpenoids . In particular, the C terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates. Or in simpler terms, the C terminal aids the synthesis of new molecules.

Structure

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It is thought to have at least two alpha helices.[1]

Conservation

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Sequences containing this protein domain belong to the terpene synthase family. It has been suggested that this gene family be designated tps (for terpene synthase). Sequence comparisons reveal similarities between the monoterpene (C10) synthases, sesquiterpene (C15) synthases and the diterpene (C20) synthases. It has been split into six subgroups on the basis of phylogeny, called Tpsa-Tpsf .[2]

See also

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Terpene synthase N terminal domain

References

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  1. ^ Starks CM, Back K, Chappell J, Noel JP (1997). "Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase". Science. 277 (5333): 1815–20. doi:10.1126/science.277.5333.1815. PMID 9295271.
  2. ^ Bohlmann J, Steele CL, Croteau R (August 1997). "Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase". J. Biol. Chem. 272 (35): 21784–92. doi:10.1074/jbc.272.35.21784. PMID 9268308.
  3. ^ [1], 5-epi- aristolochene synthase, [2] and (+)-delta-cadinene synthase SWISSPROT
  4. ^ Hyatt, D. C.; Youn, B.; Zhao, Y.; Santhamma, B.; Coates, R. M.; Croteau, R. B.; Kang, C. (2007). "4S-limonene synthase precursor - Mentha spicata (Spearmint)". Proceedings of the National Academy of Sciences of the United States of America. 104 (13). Uniprot.org: 5360–5. doi:10.1073/pnas.0700915104. PMC 1838495. PMID 17372193. S2CID 27479350. Retrieved 2012-08-02.
  5. ^ Ait-Ali, T.; Swain, S. M.; Reid, J. B.; Sun, T.; Kamiya, Y. (1997). "Ent-copalyl diphosphate synthase, chloroplastic precursor - Pisum sativum (Garden pea)". The Plant Journal: For Cell and Molecular Biology. 11 (3). Uniprot.org: 443–54. doi:10.1046/j.1365-313X.1997.11030443.x. PMID 9107034. Retrieved 2012-08-02.
  6. ^ Wildung, M. R.; Croteau, R. (1996). "Taxadiene synthase - Taxus brevifolia (Pacific yew)". The Journal of Biological Chemistry. 271 (16). Uniprot.org: 9201–4. doi:10.1074/jbc.271.16.9201. PMID 8621577. S2CID 3191132. Retrieved 2012-08-02.
  7. ^ "Pinene synthase, chloroplastic precursor - Abies grandis (Grand fir)". Uniprot.org. Retrieved 2012-08-02.
  8. ^ "Myrcene synthase, chloroplastic precursor - Abies grandis (Grand fir)". Uniprot.org. Retrieved 2012-08-02.
  9. ^ Yamaguchi, S.; Saito, T.; Abe, H.; Yamane, H.; Murofushi, N.; Kamiya, Y. (1996). "Ent-kaur-16-ene synthase, chloroplastic precursor - Cucurbita maxima (Pumpkin)". The Plant Journal: For Cell and Molecular Biology. 10 (2). Uniprot.org: 203–13. doi:10.1046/j.1365-313X.1996.10020203.x. PMID 8771778. Retrieved 2012-08-02.
  10. ^ "Linalool synthase - Clarkia concinna (Red ribbons)". Uniprot.org. Retrieved 2012-08-02.
  11. ^ Kawaide H, Imai R, Sassa T, Kamiya Y (August 1997). "Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis". J. Biol. Chem. 272 (35): 21706–12. doi:10.1074/jbc.272.35.21706. PMID 9268298.
This article incorporates text from the public domain Pfam and InterPro: IPR005630