CATH Classification

Domain Context

CATH Clusters

Superfamily Protein prenylyltransferase
Functional Family Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Enzyme Information

2.5.1.58
Protein farnesyltransferase.
based on mapping to UniProt Q04631
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
-!- This enzyme, along with EC 2.5.1.59 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. -!- Catalyzes the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. -!- These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. -!- The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. -!- Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction.
2.5.1.59
Protein geranylgeranyltransferase type I.
based on mapping to UniProt Q04631
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl- protein + diphosphate.
-!- This enzyme, along with EC 2.5.1.58 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. -!- Catalyzes the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. -!- These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. -!- The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. -!- Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. -!- The Zn(2+) is required for peptide, but not for isoprenoid, substrate binding.

UniProtKB Entries (1)

Q02293
FNTB_RAT
Rattus norvegicus
Protein farnesyltransferase subunit beta

PDB Structure

PDB 2BED
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Enhanced FTase activity achieved via piperazine interaction with catalytic zinc.
Njoroge, F.G., Vibulbhan, B., Pinto, P., Strickland, C., Bishop, W.R., Nomeir, A., Girijavallabhan, V.
Bioorg.Med.Chem.Lett.