Terpene_synth
(+)-bornyl diphosphate synthase: complex with mg and product
Identifiers
SymbolTerpene_synth
PfamPF01397
InterProIPR001906
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 N terminal domain of the TPS protein.

Function

Terpenes synthases have a role in producing important molecules in metabolism, these molecules are part of a large group called terpenoids . In particular, the N terminal domain has feature of the copalyl diphosphate synthase (CPS) active site.[1]

Structure

The N-terminal domain forms an alpha-barrel similar to that of the sesquiterpene cyclase epiaristolochene synthase.[2]

Conservation

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 .[3]

See also

Terpene synthase C terminal domain

References

  1. ^ Chen F, Tholl D, Bohlmann J, Pichersky E (2011). "The family of terpene synthases in plants: a mid-size family of genes for specialized metabolism that is highly diversified throughout the kingdom". Plant J. 66 (1): 212–29. doi:10.1111/j.1365-313X.2011.04520.x. PMID 21443633.
  2. ^ Whittington DA, Wise ML, Urbansky M, Coates RM, Croteau RB, Christianson DW (2002). "Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase". Proc Natl Acad Sci U S A. 99 (24): 15375–80. Bibcode:2002PNAS...9915375W. doi:10.1073/pnas.232591099. PMC 137724. PMID 12432096.
  3. ^ 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.
  4. ^ [1], 5-epi- aristolochene synthase, [2] and (+)-delta-cadinene synthase SWISSPROT
  5. ^ 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. Uniprot.org. 104 (13): 5360–5. doi:10.1073/pnas.0700915104. PMC 1838495. PMID 17372193. Retrieved 2012-08-02.
  6. ^ 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. Uniprot.org. 11 (3): 443–54. doi:10.1046/j.1365-313X.1997.11030443.x. PMID 9107034. Retrieved 2012-08-02.
  7. ^ Wildung, M. R.; Croteau, R. (1996). "Taxadiene synthase - Taxus brevifolia (Pacific yew)". The Journal of Biological Chemistry. Uniprot.org. 271 (16): 9201–4. doi:10.1074/jbc.271.16.9201. PMID 8621577. S2CID 3191132. Retrieved 2012-08-02.
  8. ^ "Pinene synthase, chloroplastic precursor - Abies grandis (Grand fir)". Uniprot.org. Retrieved 2012-08-02.
  9. ^ "Myrcene synthase, chloroplastic precursor - Abies grandis (Grand fir)". Uniprot.org. Retrieved 2012-08-02.
  10. ^ 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. Uniprot.org. 10 (2): 203–13. doi:10.1046/j.1365-313X.1996.10020203.x. PMID 8771778. Retrieved 2012-08-02.
  11. ^ "Linalool synthase - Clarkia concinna (Red ribbons)". Uniprot.org. Retrieved 2012-08-02.
  12. ^ 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: IPR001906
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