Prenyltransferase: Difference between revisions

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==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
SymbolPrenyltrans
PfamPF00432
InterProIPR001330
PROSITEPDOC00825
SCOP21sqc / SCOPe / SUPFAM
OPM protein1w6k
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1w6kA:122-165 1w6jA:122-165 1o6qA:59-102

1umpC:59-102 1h39A:59-102 1h3cB:59-102 2sqcA:59-102 1h37A:59-102 1o6hA:59-102 1gszA:59-102 3sqcA:59-102 1o79A:59-102 1h35A:59-102 1h3aC:59-102 1h36A:59-102 1h3bA:59-102 1o6rB:59-102 1sqc :59-102 1s64L:142-186 1tnuJ:142-186 1n4qH:142-186 1n4pD:142-186 1n4sL:142-186 1n4rH:142-186 1tnzL:142-186 1tnyL:142-186 1tnbD:142-186 1tnoH:142-186 1dceD:114-157 1ltxB:114-157 1jcqB:172-215 1mzcB:172-215 1s63B:172-215 1sa4B:172-215 1ld7B:172-215 1ld8B:172-215 1tn6B:172-215 2ftiB:172-215 1fppB:172-215 1n9aB:172-215 1nl4B:172-215 1hz7B:172-215 1o5mB:172-215 1n94B:172-215 1kzoB:172-215 1jcrB:172-215 1o1rB:172-215 1ni1B:172-215 1sa5B:172-215 1ftiB:172-215 1qbqB:172-215 1d8dB:172-215 1ft2B:172-215 1ft1B:172-215 1o1sB:172-215 1d8eB:172-215 1tn8B:172-215 1qe2B:172-215 1x81B:172-215 1kzpB:172-215 1tn7B:172-215 1kzrB:172-215 1jcsB:172-215

3ftiB:172-215 1o1tB:172-215 1n95B:172-215

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

FNTB; LSS; PGGT1B; RABGGTB

References

  1. ^ 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.
  2. ^ 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)
  3. ^ 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}}: 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)
This article incorporates text from the public domain Pfam and InterPro: IPR001330