| EC |
2.5.1.59 |
| Accepted name: |
protein geranylgeranyltransferase type I |
| Reaction: |
geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate |
| Other name(s): |
GGTase-I; GGTaseI |
| Systematic name: |
geranylgeranyl-diphosphate:protein-cysteine geranyltransferase |
| Comments: |
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 γ-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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 135371-29-8 |
| References: |
| 1. |
Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289–5292. [DOI] [PMID: 8621375] |
| 2. |
Zhang, F.L. and Casey, P.J. Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I. Biochem. J. 320 (1996) 925–932. [PMID: 9003382] |
| 3. |
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. |
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| [EC 2.5.1.59 created 2003] |
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