FTase and GGTase-I are designated CaaX prenyltransferases, since they recognize their protein substrates by the so-called CaaX-box. Both enzymes share a common α subunit (48 kDa) and a homologous β subunit (46 kDa in FTase, 42 kDa in GGTase-I). GGTase-II or RabGGTase differs from FTase and GGTase-I, both structurally and functionally. The enzyme attaches geranylgeranyl groups to two C-terminal cysteines of Rab proteins that terminate in CC or CXC motifs.
Engineered mutants of FTase (Cat.# PR-952 and PR-953) and GGTase-I (Cat.# PR-954) in combination with our innovative and universal lipid donor B-GPP (Cat.# LI-015) allow the detection of femtomolar amounts of prenylatable proteins in eukaryotic cells and tissues and thereby offer a new generation of prenylation studies.
Hougland et al. (2009) Getting a handle on protein prenylation. Nat. Chem. Biol. 5 (4):197
Nguyen et al. (2009) Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. Nat. Chem. Biol. 5 (4):227
Lane et al. (2006) Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. J. Lipid Res. 47:681
Casey et al. (1996) Protein Prenyltransferases. J. Biol. Chem. 271 (10):5289
