Prenyltransferase and squalene oxidase repeat | |||||||||
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Structure of a squalene cyclase.
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Identifiers | |||||||||
Symbol | Prenyltrans | ||||||||
Pfam | PF00432 | ||||||||
Pfam clan | CL0059 | ||||||||
InterPro | IPR001330 | ||||||||
PROSITE | PDOC00825 | ||||||||
SCOP | 1sqc | ||||||||
SUPERFAMILY | 1sqc | ||||||||
OPM superfamily | 38 | ||||||||
OPM protein | 1w6k | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Prenyltransferases are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases.
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. 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. 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.
This article incorporates text from the public domain Pfam and InterPro IPR001330