Prenyltransferase
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Prenyltransferase and squalene oxidase repeat | ||
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Identifiers | ||
Symbol | Prenyltrans | |
Pfam | PF00432 | |
InterPro | IPR001330 | |
PROSITE | PDOC00825 | |
SCOP | 1sqc | |
OPM protein | 1w6k | |
Available PDB structures:
1w6kA: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.
Contents |
[edit] Human proteins containing this domain
[edit] References
- ^ Takahashi, S. and T. Koyama. Chem Rec 2006,6(4):194-205.
- ^ Schulz GE, Wendt KU, Poralla K (1997). "Structure and function of a squalene cyclase". Science 277 (5333): 1811–1815. doi: . PMID 9295270.
- ^ 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: . PMID 8016864.
[edit] External links
[edit] Further reading
- [1]. Structure and function of a squalene cyclase. Wendt KU, Poralla K, Schulz GE; Science 1997;277:1811-1815. PubMed
- [2]. A specific amino acid repeat in squalene and oxidosqualene cyclases. Poralla K, Hewelt A, Prestwich GD, Abe I, Reipen I, Sprenger G; Trends Biochem Sci 1994;19:157-158. PubMed
This article includes text from the public domain Pfam and InterPro IPR001330