Prenyltransferase: Difference between revisions
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==Further reading== |
==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 (journal) | volume = 277 | issue = 5333 | pages = 1811–5 | year = 1997 | month = September | pmid = 9295270 | doi = 10. |
* {{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 = 10.1126/science.277.5333.1811 | url = | issn = }} |
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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 | year = 1994 | month = April | pmid = 8016864 | doi = 10.1016/0968-0004(94)90276-3| 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 = }} |
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Revision as of 18:10, 11 December 2010
Prenyltransferase and squalene oxidase repeat | |||||||||||
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Identifiers | |||||||||||
Symbol | Prenyltrans | ||||||||||
Pfam | PF00432 | ||||||||||
Pfam clan | CL0059 | ||||||||||
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.[2]
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.[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 (1997). "Structure and function of a squalene cyclase". Science. 277 (5333): 1811–5. doi:10.1126/science.277.5333.1811. PMID 9295270.
{{cite journal}}
: Unknown parameter|month=
ignored (help)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)
Further reading
- Wendt KU, Poralla K, Schulz GE (1997). "Structure and function of a squalene cyclase". Science (journal). 277 (5333): 1811–5. doi:10.1126/science.277.5333.1811. PMID 9295270.
{{cite journal}}
: Unknown parameter|month=
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. doi:10.1016/0968-0004(94)90276-3. PMID 8016864.
{{cite journal}}
: Unknown parameter|month=
ignored (help)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