Prenyltransferase: Difference between revisions

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| Symbol = Prenyltrans
| Symbol = Prenyltrans
| Name = Prenyltransferase and squalene oxidase repeat
| Name = Prenyltransferase and squalene oxidase repeat
| image =
| image = PDB 1sqc EBI.jpg
| width =
| width =
⚫
| caption = Structure of a squalene cyclase.<ref name="pmid9295270">{{cite journal |vauthors=Wendt KU, Poralla K, Schulz GE |title=Structure and function of a squalene cyclase |journal=Science |volume=277 |issue=5333 |pages=1811–1815 |date=1997 |pmid=9295270 |doi= 10.1126/science.277.5333.1811}}</ref>
| caption =
| Pfam= PF00432
| Pfam= PF00432
| Pfam_clan= CL0059
| InterPro= IPR001330
| InterPro= IPR001330
| SMART=
| SMART=
Line 11: Line 12:
| SCOP = 1sqc
| SCOP = 1sqc
| TCDB =
| TCDB =
| OPM family=
| OPM family= 37
| OPM protein= 1w6k
| OPM protein= 1w6k
| PDB=
| PDB=
{{PDB3|1w6k}}A:122-165 {{PDB3|1w6j}}A:122-165 {{PDB3|1o6q}}A:59-102
{{PDB3|1ump}}C:59-102 {{PDB3|1h39}}A:59-102 {{PDB3|1h3c}}B:59-102
{{PDB3|2sqc}}A:59-102 {{PDB3|1h37}}A:59-102 {{PDB3|1o6h}}A:59-102
{{PDB3|1gsz}}A:59-102 {{PDB3|3sqc}}A:59-102 {{PDB3|1o79}}A:59-102
{{PDB3|1h35}}A:59-102 {{PDB3|1h3a}}C:59-102 {{PDB3|1h36}}A:59-102
{{PDB3|1h3b}}A:59-102 {{PDB3|1o6r}}B:59-102 {{PDB3|1sqc}} :59-102
{{PDB3|1s64}}L:142-186 {{PDB3|1tnu}}J:142-186 {{PDB3|1n4q}}H:142-186
{{PDB3|1n4p}}D:142-186 {{PDB3|1n4s}}L:142-186 {{PDB3|1n4r}}H:142-186
{{PDB3|1tnz}}L:142-186 {{PDB3|1tny}}L:142-186 {{PDB3|1tnb}}D:142-186
{{PDB3|1tno}}H:142-186 {{PDB3|1dce}}D:114-157 {{PDB3|1ltx}}B:114-157
{{PDB3|1jcq}}B:172-215 {{PDB3|1mzc}}B:172-215 {{PDB3|1s63}}B:172-215
{{PDB3|1sa4}}B:172-215 {{PDB3|1ld7}}B:172-215 {{PDB3|1ld8}}B:172-215
{{PDB3|1tn6}}B:172-215 {{PDB3|2fti}}B:172-215 {{PDB3|1fpp}}B:172-215
{{PDB3|1n9a}}B:172-215 {{PDB3|1nl4}}B:172-215 {{PDB3|1hz7}}B:172-215
{{PDB3|1o5m}}B:172-215 {{PDB3|1n94}}B:172-215 {{PDB3|1kzo}}B:172-215
{{PDB3|1jcr}}B:172-215 {{PDB3|1o1r}}B:172-215 {{PDB3|1ni1}}B:172-215
{{PDB3|1sa5}}B:172-215 {{PDB3|1fti}}B:172-215 {{PDB3|1qbq}}B:172-215
{{PDB3|1d8d}}B:172-215 {{PDB3|1ft2}}B:172-215 {{PDB3|1ft1}}B:172-215
{{PDB3|1o1s}}B:172-215 {{PDB3|1d8e}}B:172-215 {{PDB3|1tn8}}B:172-215
{{PDB3|1qe2}}B:172-215 {{PDB3|1x81}}B:172-215 {{PDB3|1kzp}}B:172-215
{{PDB3|1tn7}}B:172-215 {{PDB3|1kzr}}B:172-215 {{PDB3|1jcs}}B:172-215
{{PDB3|3fti}}B:172-215 {{PDB3|1o1t}}B:172-215 {{PDB3|1n95}}B:172-215
}}
}}
'''Prenyltransferases''' are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases.<ref name="pmid16900467">{{cite journal | author = Takahashi S, Koyama T | title = Structure and function of cis-prenyl chain elongating enzymes | journal = Chem Rec | volume = 6 | issue = 4 | pages = 194–205 | year = 2006 | pmid = 16900467 | doi = 10.1002/tcr.20083 | url = | issn = }}</ref>
'''Prenyltransferases''' (PTs) are a class of [[enzyme]]s that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to isoprenyl diphosphate syntheses (IPPSs).<ref name="pmid16900467">{{cite journal |vauthors=Takahashi S, Koyama T | title = Structure and function of cis-prenyl chain elongating enzymes | journal = The Chemical Record | volume = 6 | issue = 4 | pages = 194–205 | year = 2006 | pmid = 16900467 | doi = 10.1002/tcr.20083 | doi-access = free }}</ref><ref>{{Cite journal |last1=Liang |first1=Po-Huang |last2=Ko |first2=Tzu-Ping |last3=Wang |first3=Andrew H.-J |date=July 2002 |title=Structure, mechanism and function of prenyltransferases: Structure, mechanism and function of prenyltransferases |url=http://doi.wiley.com/10.1046/j.1432-1033.2002.03014.x |journal=European Journal of Biochemistry |language=en |volume=269 |issue=14 |pages=3339–3354 |doi=10.1046/j.1432-1033.2002.03014.x|pmid=12135472 }}</ref> Prenyltransferases are a functional category and include several enzyme groups that are evolutionarily independent.


Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the stereo chemistry of the resulting products. Examples of trans-prenyltranferases include [[dimethylallyltranstransferase]], and geranylgeranyl pyrophosphate synthase. Cis-prenyltransferases include dehydrodolichol diphosphate synthase (involved in the production of a precursor to [[dolichol]]).
Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the [[stereochemistry]] of the resulting products. Examples of trans-prenyltranferases include [[dimethylallyltranstransferase]], and geranylgeranyl pyrophosphate synthase. Cis-prenyltransferases include [[dehydrodolichol diphosphate synthase]] (involved in the production of a precursor to [[dolichol]]). Trans- and cis-prenyltransferases are evolutionarily unrelated to each other and there is no sequential and structural similarity.


The beta subunit of the [[farnesyltransferase]]s is responsible for peptide binding. Squalene-hopene cyclase is a bacterial enzyme that catalyzes the cyclization of squalene into hopene, a key step in hopanoid (triterpenoid) metabolism.<ref name="PUB00005227">{{cite journal |author=Schulz GE, Wendt KU, Poralla K |title=Structure and function of a squalene cyclase |journal=Science |volume=277 |issue=5333 |pages=1811–1815 |year=1997 |pmid=9295270 |doi=10.1126/science.277.5333.1811}}</ref> Lanosterol synthase ({{EC number|5.4.99.7}}) (oxidosqualene-lanosterol cyclase) catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormones and vitamin D in vertebrates and of ergosterol in fungi.<ref name="PUB00005416">{{cite journal |author=Prestwich GD, Poralla K, Hewelt A, Abe I, Reipen I, Sprenger G |title=A specific amino acid repeat in squalene and oxidosqualene cyclases |journal=Trends Biochem. Sci. |volume=19 |issue=4 |pages=157–158 |year=1994 |pmid=8016864 |doi=10.1016/0968-0004(94)90276-3}}</ref> Cycloartenol synthase ({{EC number| 5.4.99.8}}) (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (S)-2,3-epoxysqualene to cycloartenol.
The beta subunit of the [[farnesyltransferase]]s is responsible for peptide binding. [[Squalene-hopene cyclase]] is a bacterial enzyme that catalyzes the [[cyclization reaction|cyclization]] of [[squalene]] into [[hopene]], a key step in hopanoid ([[triterpenoid]]) metabolism.<ref name="pmid9295270">{{cite journal |vauthors=Wendt KU, Poralla K, Schulz GE |title=Structure and function of a squalene cyclase |journal=Science |volume=277 |issue=5333 |pages=1811–1815 |date=1997 |pmid=9295270 |doi= 10.1126/science.277.5333.1811}}</ref> [[Lanosterol synthase]] ({{EC number|5.4.99.7}}) (oxidosqualene-lanosterol cyclase) catalyzes the cyclization of [[(S)-2,3-epoxysqualene|(''S'')-2,3-epoxysqualene]] to [[lanosterol]], the initial precursor of [[cholesterol]], [[steroid hormone]]s and vitamin D in vertebrates and of [[ergosterol]] in fungi.<ref name="PUB00005416">{{cite journal |vauthors=Prestwich GD, Poralla K, Hewelt A, Abe I, Reipen I, Sprenger G |title=A specific amino acid repeat in squalene and oxidosqualene cyclases |journal=Trends Biochem. Sci. |volume=19 |issue=4 |pages=157–158 |year=1994 |pmid=8016864 |doi=10.1016/0968-0004(94)90276-3}}</ref> [[Cycloartenol synthase]] ({{EC number|5.4.99.8}}) (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (''S'')-2,3-epoxysqualene to [[cycloartenol]].


==Human proteins containing this domain ==
==Human proteins containing this domain ==
[[FNTB]]; [[LSS (gene)|LSS]]; [[PGGT1B]]; [[RABGGTB]]
[[FNTB]]; [[Lanosterol synthase|LSS]]; [[Geranylgeranyltransferase type 1|PGGT1B]]; [[Rab geranylgeranyltransferase|RABGGTB]]

==See also==
* [[Cis–trans isomerism|''Cis''–''trans'' isomerism]]
* [[E–Z notation|''E''–''Z'' notation]]


==References==
==References==
{{reflist}}
{{reflist|30em}}


==External links==
==External links==
⚫
* [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC00703 Protein prenyltransferases alpha subunit repeat] in [[PROSITE]]
* {{MeshName|Prenyltransferase}}
* {{MeshName|Prenyltransferase}}
⚫
* [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC00703 Protein prenyltransferases alpha subunit repeat] in [[PROSITE]]

==Further reading==
⚫
* {{cite journal | author = Wendt KU, Poralla K, Schulz GE | title = Structure and function of a squalene cyclase | journal = Science (journal) | volume = 277 | issue = 5333 | pages = 1811–5 | year = 1997 | month = September | pmid = 9295270 | doi = 10.1002/tcr.20083 | url = | issn = }}
* {{cite journal | author = Poralla K, Hewelt A, Prestwich GD, Abe I, Reipen I, Sprenger G | title = A specific amino acid repeat in squalene and oxidosqualene cyclases | journal = Trends Biochem. Sci. | volume = 19 | issue = 4 | pages = 157–8 | year = 1994 | month = April | pmid = 8016864 | doi = 10.1016/0968-0004(94)90276-3| url = | issn = }}


{{InterPro content|IPR001330}}
{{InterPro content|IPR001330}}


{{Alkyl and aryl transferases}}
⚫
{{enzyme-stub}}


[[Category:Peripheral membrane proteins]]
[[Category:Peripheral membrane proteins]]
[[Category:Protein domains]]
[[Category:Protein domains]]


⚫
{{enzyme-stub}}

Latest revision as of 03:29, 22 February 2024

Prenyltransferase and squalene oxidase repeat
Structure of a squalene cyclase.[1]
Identifiers
SymbolPrenyltrans
PfamPF00432
Pfam clanCL0059
InterProIPR001330
PROSITEPDOC00825
SCOP21sqc / SCOPe / SUPFAM
OPM superfamily37
OPM protein1w6k
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Prenyltransferases (PTs) are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to isoprenyl diphosphate syntheses (IPPSs).[2][3] Prenyltransferases are a functional category and include several enzyme groups that are evolutionarily independent.

Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the stereochemistry of the resulting products. Examples of trans-prenyltranferases include dimethylallyltranstransferase, and geranylgeranyl pyrophosphate synthase. Cis-prenyltransferases include dehydrodolichol diphosphate synthase (involved in the production of a precursor to dolichol). Trans- and cis-prenyltransferases are evolutionarily unrelated to each other and there is no sequential and structural similarity.

The beta subunit of the farnesyltransferases is responsible for peptide binding. Squalene-hopene cyclase is a bacterial enzyme that catalyzes the cyclization of squalene into hopene, a key step in hopanoid (triterpenoid) metabolism.[1] Lanosterol synthase (EC 5.4.99.7) (oxidosqualene-lanosterol cyclase) catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormones and vitamin D in vertebrates and of ergosterol in fungi.[4] Cycloartenol synthase (EC 5.4.99.8) (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (S)-2,3-epoxysqualene to cycloartenol.

Human proteins containing this domain[edit]

FNTB; LSS; PGGT1B; RABGGTB

See also[edit]

References[edit]

  1. ^ a b Wendt KU, Poralla K, Schulz GE (1997). "Structure and function of a squalene cyclase". Science. 277 (5333): 1811–1815. doi:10.1126/science.277.5333.1811. PMID 9295270.
  2. ^ Takahashi S, Koyama T (2006). "Structure and function of cis-prenyl chain elongating enzymes". The Chemical Record. 6 (4): 194–205. doi:10.1002/tcr.20083. PMID 16900467.
  3. ^ Liang, Po-Huang; Ko, Tzu-Ping; Wang, Andrew H.-J (July 2002). "Structure, mechanism and function of prenyltransferases: Structure, mechanism and function of prenyltransferases". European Journal of Biochemistry. 269 (14): 3339–3354. doi:10.1046/j.1432-1033.2002.03014.x. PMID 12135472.
  4. ^ Prestwich GD, Poralla K, Hewelt A, Abe I, Reipen I, Sprenger G (1994). "A specific amino acid repeat in squalene and oxidosqualene cyclases". Trends Biochem. Sci. 19 (4): 157–158. doi:10.1016/0968-0004(94)90276-3. PMID 8016864.

External links[edit]

This article incorporates text from the public domain Pfam and InterPro: IPR001330


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