2.5.1.59	farnesyl diphosphate + protein-cysteine	the enzyme catalyzes postttranslational modification of proteins, the farnesyl moieties attached to the substrates are direcly involved in protein-protein interactions as well as in protein-membrane interactions	
2.5.1.59	geranylgeranyl diphosphate + Cdc42-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + Cdc420-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + K Ras-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + N-Ras-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + protein-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + protein-cysteine	enzyme catalyses the transfer of the 20-carbon prenyl group from geranylgeranyl diphosphate to the cysteine residue near the C-termini of a variety of eukaryotic proteins	
2.5.1.59	geranylgeranyl diphosphate + protein-cysteine	this prenylation is necessary for many proteins to interact with membrane localized at proper intracellular sites	
2.5.1.59	geranylgeranyl diphosphate + protein-cysteine	yeast enzyme is essential for yeast cell growth	
2.5.1.59	geranylgeranyl diphosphate + protein-cysteine	GGTase-I catalyzes C-terminal lipidation of more than 100 proteins, including many GTP-binding regulatory proteins	
2.5.1.59	geranylgeranyl diphosphate + protein-cysteine	the enzyme negatively regulates abscisic acid signaling in guard cells. The enzyme is specifically involved in negative regulation of auxin-induced lateral root initiation	
2.5.1.59	geranylgeranyl diphosphate + protein-cysteine	the enzyme adds a C20 geranylgeranyl group to proteins such as RhoA, RhoC, Rap1 and Ral at the cysteine within the carboxy-terminal tetrapeptide consensus sequence CAAL (C is cysteine, A is an aliphatic amino acid, and the C-terminal residue is leucine or phenylalanine)	
2.5.1.59	geranylgeranyl diphosphate + protein-cysteine	the enzyme catalyzes posttranslational modification of proteins, the farnesyl moieties attached to the substrates are direcly involved in protein-protein interactions as well as in protein-membrane interactions	
2.5.1.59	geranylgeranyl diphosphate + Rac GTPase-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + Rac-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + Rap-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + Rap1A-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + Ras protein	-	
2.5.1.59	geranylgeranyl diphosphate + Ras-CVLL	tritium labelled geranylgeranyl diphosphate for enzyme assay, His-tagged geranylgeranyl diphosphate	
2.5.1.59	geranylgeranyl diphosphate + Rho GTPase-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + Rho-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + Rho10-cysteine	-	
2.5.1.59	geranylgeranyl diphosphate + RhoA GTPase-cysteine	-	
2.5.1.59	additional information	the enzyme modifies proteins by attaching a 20-carbon isoprenoid group to a cysteine residue near the C-terminus of a target protein. The enzyme requires a C-terminal Ca1a2X sequence on its substrates, with the a1, a2, and X residues serving as substrate-recognition elements for GGTase-I. Crystallographic structures of rat GGTase-I show a tightly packed and hydrophobic a2 residue binding pocket, consistent with a preference for moderately sized a2 residues in GGTase-I substrates, peptide substrate structure-activity relationship, overview. Identification of specific active-site residues within rat GGTase-I involved in substrate recognition