Prenyltransferase: Difference between revisions
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==References== |
==References== |
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==Further reading== |
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* {{cite journal | author = Wendt KU, Poralla K, Schulz GE | title = Structure and function of a squalene cyclase | journal = Science | volume = 277 | issue = 5333 | pages = 1811–5 |date=September 1997 | pmid = 9295270 | doi = 10.1126/science.277.5333.1811 | url = }} |
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* {{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 |date=April 1994 | pmid = 8016864 | doi = 10.1016/0968-0004(94)90276-3| url = }} |
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==External links== |
==External links== |
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Revision as of 02:49, 17 November 2015
| Prenyltransferase and squalene oxidase repeat | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of a squalene cyclase.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Prenyltrans | ||||||||
| Pfam | PF00432 | ||||||||
| Pfam clan | CL0059 | ||||||||
| InterPro | IPR001330 | ||||||||
| PROSITE | PDOC00825 | ||||||||
| SCOP2 | 1sqc / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 38 | ||||||||
| 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.[2]
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).
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.[3] 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
References
- ^ Wendt KU, Poralla K, Schulz GE (September 1997). "Structure and function of a squalene cyclase". Science. 277 (5333): 1811–5. doi:10.1126/science.277.5333.1811. PMID 9295270.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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
- Prenyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Protein prenyltransferases alpha subunit repeat in PROSITE
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