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 = 10.1002/tcr.20083 | url = | issn = }}
* {{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 = }}
* {{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
Structure of a squalene cyclase.[1]
Identifiers
SymbolPrenyltrans
PfamPF00432
Pfam clanCL0059
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.[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

FNTB; LSS; PGGT1B; RABGGTB

References

  1. ^ 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)
  2. ^ 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.
  3. ^ 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)
  4. ^ 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

External links


This article incorporates text from the public domain Pfam and InterPro: IPR001330