Terpene synthase N terminal domain
{{short description|Protein domain}}
{{Infobox protein family
| Symbol = Terpene_synth
| Name = Terpene_synth
| image = PDB 1n24 EBI.jpg
| width =
| caption = (+)-bornyl diphosphate synthase: complex with mg and product
| Pfam = PF01397
| Pfam_clan =
| InterPro = IPR001906
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 5eau
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
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.{{cite journal|vauthors=Chen F, Tholl D, Bohlmann J, Pichersky E | title=The family of terpene synthases in plants: a mid-size family of genes for specialized metabolism that is highly diversified throughout the kingdom. | journal=Plant J | year= 2011 | volume= 66 | issue= 1 | pages= 212–29 | pmid=21443633 | doi=10.1111/j.1365-313X.2011.04520.x | doi-access=free }}
Structure
The N-terminal domain forms an alpha-barrel similar to that of the sesquiterpene cyclase epiaristolochene synthase.{{cite journal|author6-link=David W. Christianson|vauthors=Whittington DA, Wise ML, Urbansky M, Coates RM, Croteau RB, Christianson DW | title=Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase. | journal=Proc Natl Acad Sci U S A | year= 2002 | volume= 99 | issue= 24 | pages= 15375–80 | pmid=12432096 | doi=10.1073/pnas.232591099 | pmc=137724 | bibcode=2002PNAS...9915375W | doi-access=free }}
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 .{{cite journal |vauthors=Bohlmann J, Steele CL, Croteau R | title = Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase | journal = J. Biol. Chem. | volume = 272 | issue = 35 | pages = 21784–92 |date=August 1997 | pmid = 9268308 | doi = 10.1074/jbc.272.35.21784| doi-access = free }}
- Tpsa includes vetispiridiene synthase.[https://www.uniprot.org/uniprot/Q39979], 5-epi- aristolochene synthase, [https://www.uniprot.org/uniprot/Q40577] and (+)-delta-cadinene synthase [https://www.uniprot.org/uniprot/P93665 SWISSPROT]
- Tpsb includes (-)-limonene synthase.{{cite journal|url=https://www.uniprot.org/uniprot/Q40322 |title=4S-limonene synthase precursor - Mentha spicata (Spearmint) |year=2007 |doi=10.1073/pnas.0700915104 |publisher=Uniprot.org |pmid=17372193 |access-date=2012-08-02|last1=Hyatt |first1=D. C. |last2=Youn |first2=B. |last3=Zhao |first3=Y. |last4=Santhamma |first4=B. |last5=Coates |first5=R. M. |last6=Croteau |first6=R. B. |last7=Kang |first7=C. |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=104 |issue=13 |pages=5360–5 |pmc=1838495 |doi-access=free }}
- Tpsc includes copalyl diphosphate synthase (kaurene synthase A).{{cite journal|url=https://www.uniprot.org/uniprot/O04408 |title=Ent-copalyl diphosphate synthase, chloroplastic precursor - Pisum sativum (Garden pea) |year=1997 |doi=10.1046/j.1365-313X.1997.11030443.x |publisher=Uniprot.org |pmid=9107034 |access-date=2012-08-02|last1=Ait-Ali |first1=T. |last2=Swain |first2=S. M. |last3=Reid |first3=J. B. |last4=Sun |first4=T. |last5=Kamiya |first5=Y. |journal=The Plant Journal: For Cell and Molecular Biology |volume=11 |issue=3 |pages=443–54 |doi-access=free }}
- Tpsd includes taxadiene synthase,{{cite journal|url=https://www.uniprot.org/uniprot/Q41594 |title=Taxadiene synthase - Taxus brevifolia (Pacific yew) |year=1996 |doi=10.1074/jbc.271.16.9201 |publisher=Uniprot.org |pmid=8621577 |access-date=2012-08-02|last1=Wildung |first1=M. R. |last2=Croteau |first2=R. |journal=The Journal of Biological Chemistry |volume=271 |issue=16 |pages=9201–4 |s2cid=3191132 |doi-access=free }} pinene synthase,{{cite web|url=https://www.uniprot.org/uniprot/O24475 |title=Pinene synthase, chloroplastic precursor - Abies grandis (Grand fir) |publisher=Uniprot.org |access-date=2012-08-02}} and myrcene synthase.{{cite web|url=https://www.uniprot.org/uniprot/O24474 |title=Myrcene synthase, chloroplastic precursor - Abies grandis (Grand fir) |publisher=Uniprot.org |access-date=2012-08-02}}
- Tpse includes ent-kaurene synthase B.{{cite journal|url=https://www.uniprot.org/uniprot/Q39548 |title=Ent-kaur-16-ene synthase, chloroplastic precursor - Cucurbita maxima (Pumpkin) |year=1996 |doi=10.1046/j.1365-313X.1996.10020203.x |publisher=Uniprot.org |pmid=8771778 |access-date=2012-08-02|last1=Yamaguchi |first1=S. |last2=Saito |first2=T. |last3=Abe |first3=H. |last4=Yamane |first4=H. |last5=Murofushi |first5=N. |last6=Kamiya |first6=Y. |journal=The Plant Journal: For Cell and Molecular Biology |volume=10 |issue=2 |pages=203–13 |url-access=subscription }}
- Tpsf includes S-linalool synthase.{{cite web|url=https://www.uniprot.org/uniprot/Q9ZPN5 |title=Linalool synthase - Clarkia concinna (Red ribbons) |publisher=Uniprot.org |access-date=2012-08-02}} In the fungus Phaeosphaeria sp. (strain L487) the synthesis of ent-kaurene from geranylgeranyl dophosphate is promoted by a single bifunctional protein.{{cite journal |vauthors=Kawaide H, Imai R, Sassa T, Kamiya Y | title = Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis | journal = J. Biol. Chem. | volume = 272 | issue = 35 | pages = 21706–12 |date=August 1997 | pmid = 9268298 | doi = 10.1074/jbc.272.35.21706| doi-access = free }}