Terpene synthase N terminal domain

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Terpene_synth
PDB 1n24 EBI.jpg
(+)-bornyl diphosphate synthase: complex with mg and product
Identifiers
SymbolTerpene_synth
Pfam PF01397
InterPro IPR001906
SCOP2 5eau / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure 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.

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 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

Related Research Articles

Gibberellins (GAs) are plant hormones that regulate various developmental processes, including stem elongation, germination, dormancy, flowering, flower development, and leaf and fruit senescence. GAs are one of the longest-known classes of plant hormone. It is thought that the selective breeding of crop strains that were deficient in GA synthesis was one of the key drivers of the "green revolution" in the 1960s, a revolution that is credited to have saved over a billion lives worldwide.

<span class="mw-page-title-main">Bornyl diphosphate synthase</span>

In enzymology, bornyl diphosphate synthase (BPPS) (EC 5.5.1.8) is an enzyme that catalyzes the chemical reaction

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

In enzymology, an ent-copalyl diphosphate synthase is an enzyme that catalyzes the chemical reaction:

The enzyme (4S)-limonene synthase catalyzes the chemical reaction

The enzyme ent-kaurene synthase catalyzes the chemical reaction

The enzyme myrcene synthase catalyzes the chemical reaction

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

<span class="mw-page-title-main">Terpene synthase C terminal domain</span> 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 C terminal domain of the TPS protein.

ent-Cassa-12,15-diene synthase is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase (ent-cassa-12,15-diene-forming). This enzyme catalyses the following chemical reaction

ent-Sandaracopimaradiene synthase is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase [ent-sandaracopimara-8(14),15-diene-forming]. This enzyme catalyses the following chemical reaction

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

(+)-Car-3-ene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-car-3-ene-forming]. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">1,8-cineole synthase</span>

1,8-Cineole synthase (EC 4.2.3.108, 1,8-cineole cyclase, geranyl pyrophoshate:1,8-cineole cyclase, 1,8-cineole synthetase) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase (cyclizing, 1,8-cineole-forming). 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

(–)-camphene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-camphene-forming]. This enzyme catalyses the following chemical reaction

(–)-α-Pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-α-pinene-forming]. This enzyme catalyses the following chemical reaction

(–)-β-Pinene synthase (EC 4.2.3.120, β-geraniolene synthase, (–)-(1S,5S)-pinene synthase, geranyldiphosphate diphosphate lyase (pinene forming)) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-β-pinene-forming]. This enzyme catalyses the following chemical reaction

(+)-α-pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-pinene-forming]. This enzyme catalyses the following chemical reaction

(+)-β-Pinene synthase is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase [(+)-β-pinene-forming]. This enzyme catalyses the following chemical reaction

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. , 5-epi- aristolochene synthase, 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