CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

2.5.1.59
Protein geranylgeranyltransferase type I.
based on mapping to UniProt P49354
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.
2.5.1.58
Protein farnesyltransferase.
based on mapping to UniProt P49354
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.

UniProtKB Entries (1)

P49356
FNTB_HUMAN
Homo sapiens
Protein farnesyltransferase subunit beta

PDB Structure

PDB 3E37
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase.
Hast, M.A., Fletcher, S., Cummings, C.G., Pusateri, E.E., Blaskovich, M.A., Rivas, K., Gelb, M.H., Van Voorhis, W.C., Sebti, S.M., Hamilton, A.D., Beese, L.S.
Chem.Biol.
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