Prenyltransferase

Prenyltransferases are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases.[2]

Prenyltransferase and squalene oxidase repeat
Structure of a squalene cyclase.[1]
Identifiers
SymbolPrenyltrans
PfamPF00432
Pfam clanCL0059
InterProIPR001330
PROSITEPDOC00825
SCOP21sqc / SCOPe / SUPFAM
OPM superfamily37
OPM protein1w6k

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.[1] 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) (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): 1811–1815. doi:10.1126/science.277.5333.1811. PMID 9295270.
  2. Takahashi S, Koyama T (2006). "Structure and function of cis-prenyl chain elongating enzymes". The Chemical Record. 6 (4): 194–205. doi:10.1002/tcr.20083. PMID 16900467.
  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.
This article incorporates text from the public domain Pfam and InterPro: IPR001330


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