Prenyltransferase: Difference between revisions
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'''Prenyltransferases''' are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases. |
'''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> |
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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 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]]). |
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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<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> |
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.<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. |
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==Human proteins containing this domain == |
==Human proteins containing this domain == |
Revision as of 10:38, 14 July 2008
Prenyltransferase and squalene oxidase repeat | |||||||||||
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Identifiers | |||||||||||
Symbol | Prenyltrans | ||||||||||
Pfam | PF00432 | ||||||||||
InterPro | IPR001330 | ||||||||||
PROSITE | PDOC00825 | ||||||||||
SCOP2 | 1sqc / SCOPe / SUPFAM | ||||||||||
OPM protein | 1w6k | ||||||||||
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Prenyltransferases are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases.[1]
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).
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.[2] 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.[3] Cycloartenol synthase (EC 5.4.99.8 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
References
- ^ Takahashi S, Koyama T (2006). "Structure and function of cis-prenyl chain elongating enzymes". Chem Rec. 6 (4): 194–205. doi:10.1002/tcr.20083. PMID 16900467.
- ^ Schulz GE, Wendt KU, Poralla K (1997). "Structure and function of a squalene cyclase". Science. 277 (5333): 1811–1815. doi:10.1126/science.277.5333.1811. PMID 9295270.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}
: CS1 maint: multiple names: authors list (link)
External links
Further reading
- Wendt KU, Poralla K, Schulz GE (1997). "Structure and function of a squalene cyclase". Science (journal). 277 (5333): 1811–5. doi:10.1002/tcr.20083. PMID 9295270.
{{cite journal}}
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ignored (help)CS1 maint: multiple names: authors list (link) - Poralla K, Hewelt A, Prestwich GD, Abe I, Reipen I, Sprenger G (1994). "A specific amino acid repeat in squalene and oxidosqualene cyclases". Trends Biochem. Sci. 19 (4): 157–8. PMID 8016864.
{{cite journal}}
: Unknown parameter|month=
ignored (help)CS1 maint: multiple names: authors list (link)