Prenyltransferase: Difference between revisions
→Human proteins containing this domain: LSS (disambiguation page) -> LSS (gene) |
→External links: mesh |
||
Line 51: | Line 51: | ||
==External links== |
==External links== |
||
* [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC00703 Protein prenyltransferases alpha subunit repeat] in [[PROSITE]] |
* [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC00703 Protein prenyltransferases alpha subunit repeat] in [[PROSITE]] |
||
* {{MeshName|Prenyltransferase}} |
|||
==Further reading== |
==Further reading== |
Revision as of 14:07, 24 February 2009
Prenyltransferase and squalene oxidase repeat | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||||
Symbol | Prenyltrans | ||||||||||
Pfam | PF00432 | ||||||||||
InterPro | IPR001330 | ||||||||||
PROSITE | PDOC00825 | ||||||||||
SCOP2 | 1sqc / SCOPe / SUPFAM | ||||||||||
OPM protein | 1w6k | ||||||||||
|
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
- Protein prenyltransferases alpha subunit repeat in PROSITE
- Prenyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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}}
: 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. PMID 8016864.
{{cite journal}}
: Unknown parameter|month=
ignored (help)CS1 maint: multiple names: authors list (link)