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2.5.1.59: protein geranylgeranyltransferase type I

This is an abbreviated version!
For detailed information about protein geranylgeranyltransferase type I, go to the full flat file.

Word Map on EC 2.5.1.59

Reaction

geranylgeranyl diphosphate
+
protein-cysteine
=
S-geranylgeranyl-protein
+
diphosphate

Synonyms

CAAX geranylgeranyltransferase, CaaX prenyltransferase, CaGGTase-I, CDC43, geranylgeranyl protein transferase type I, geranylgeranyltransferase I, geranylgeranyltransferase type I, geranylgeranyltransferase type-I, geranylgeranyltransferase-1, geranylgeranyltransferase-I, geranylgeranyltransferaseI, GGT, GGT I, GGTalpha, GGTase, GGTase I, Ggtase-1, GGTase-I, GGTaseI, GGTbeta, GGTI, mammalian GGTase-I, PGGT, PGGT beta, PGGT I, PGGT-I, PGGTase-I, PGGTaseI, Ppggb, protein geranylgeranyltransferase, protein geranylgeranyltransferase I, protein geranylgeranyltransferase type I, protein geranylgeranyltransferase type-I, protein geranylgeranyltransferase-I, type I protein geranylgeranyltransferase

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.59 protein geranylgeranyltransferase type I

Systematic Name

Systematic Name on EC 2.5.1.59 - protein geranylgeranyltransferase type I

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SYSTEMATIC NAME
IUBMB Comments
geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses 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 CA1A2X, 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 A1, but cannot act if A2 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. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.