The Enzyme Database

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Accepted name: protein geranylgeranyltransferase type II
Reaction: geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Other name(s): GGTaseII; Rab geranylgeranyltransferase; RabGGTase; geranylgeranyl-diphosphate,geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Systematic name: geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Comments: This enzyme, along with protein farnesyltransferase (EC and protein geranylgeranyltransferase type I (EC, constitutes the protein prenyltransferase family of enzymes. Attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family (Ypt/Sec4 in lower eukaryotes) that terminate in XXCC, XCXC and CCXX motifs. Reaction is entirely dependent on the Rab substrate being bound to Rab escort protein (REP). Post-translational modification with the geranylgeranyl moiety is essential for Rab GTPases to be able to control the processes of membrane docking and fusion [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 135371-29-8
1.  Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289–5292. [DOI] [PMID: 8621375]
2.  Wilson, A.L., Erdman, R.A., Castellano, F. and Maltese, W.A. Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases. Biochem. J. 333 (1998) 497–504. [PMID: 9677305]
3.  Zhang, H., Seabra, M.C. and Deisenhofer, J. Crystal structure of Rab geranylgeranyltransferase at 2.0 Å resolution. Structure 8 (2000) 241–251. [PMID: 10745007]
4.  Thomä, N.H., Niculae, A., Goody, R.S. and Alexandrov, K. Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate. J. Biol. Chem. 276 (2001) 48631–48636. [DOI] [PMID: 11591706]
5.  Rak, A., Niculae, A., Kalinin, A., Thomä, N.H., Sidorovitch, V., Goody, R.S. and Alexandrov, K. In vitro assembly, purification, and crystallization of the Rab geranylgeranyl transferase:substrate complex. Protein Expr. Purif. 25 (2002) 23–30. [DOI] [PMID: 12071695]
6.  Gibbs, R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, pp. 31–118.
[EC created 2003]

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