Terpene synthase C terminal domain

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Terpene_synth_C
PDB 5eau EBI.jpg
5-epi-aristolochene synthase from nicotiana tabacum
Identifiers
SymbolTerpene_synth_C
Pfam PF03936
InterPro IPR005630
SCOP2 5eau / SCOPe / SUPFAM

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.

Contents

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 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

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

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 . [2]

See also

Terpene synthase N terminal domain

Related Research Articles

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Terpenes are a class of natural products consisting of compounds with the formula (C5H8)n. Comprising more than 30,000 compounds, these unsaturated hydrocarbons are produced predominantly by plants, particularly conifers. Terpenes are further classified by the number of carbons: monoterpenes (C10), sesquiterpenes (C15), diterpenes (C20), etc. A well known monoterpene is alpha-pinene, a major component of turpentine.

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In enzymology, a (4S)-limonene synthase is an enzyme that catalyzes the chemical reaction

In enzymology, an ent-kaurene synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a myrcene synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a pinene synthase is an enzyme that catalyzes the chemical reaction

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Terpene synthase N terminal domain Protein domain

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.

Isopimara-7,15-diene synthase is an enzyme with systematic name (+)-copalyl diphosphate-lyase (isopimara-7,15-diene-forming). This enzyme catalyses the following chemical reaction

Gamma-humulene synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase (gamma-humulene-forming). This enzyme catalyses the following chemical reaction

Tricyclene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

Terpinolene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

Gamma-terpinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

(-)-camphene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

(-)-alpha-pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

(-)-beta-pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

(+)-alpha-pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

Neoabietadiene synthase is an enzyme with systematic name (+)-copaly-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction:

References

  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. ↑ , 5-epi- aristolochene synthase, 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. Uniprot.org. 104 (13): 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. Uniprot.org. 11 (3): 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. Uniprot.org. 271 (16): 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. Uniprot.org. 10 (2): 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.
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