Prenyltransferase

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Prenyltransferase and squalene oxidase repeat

Structure of a squalene cyclase.[1]
Identifiers
Symbol Prenyltrans
Pfam PF00432
Pfam clan CL0059
InterPro IPR001330
PROSITE PDOC00825
SCOP 1sqc
SUPERFAMILY 1sqc
OPM superfamily 38
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.[2]

Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the stereochemistry 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 (September 1997). "Structure and function of a squalene cyclase". Science 277 (5333): 1811–5. doi:10.1126/science.277.5333.1811. PMID 9295270. 
  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. 
  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. 

Further reading

  • Wendt KU, Poralla K, Schulz GE (September 1997). "Structure and function of a squalene cyclase". Science 277 (5333): 1811–5. doi:10.1126/science.277.5333.1811. PMID 9295270. 
  • Poralla K, Hewelt A, Prestwich GD, Abe I, Reipen I, Sprenger G (April 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. 

External links


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

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