Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cd2+ | the zinc in enzyme can be replaced by Cd2+ | Saccharomyces cerevisiae | |
Mg2+ | no requirement | Saccharomyces cerevisiae | |
Zn2+ | A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
43000 | - |
alpha,beta, 1 * 48000 + 1 * 43000 | Saccharomyces cerevisiae |
48000 | - |
alpha,beta, 1 * 48000 + 1 * 43000 | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
geranylgeranyl diphosphate + protein-cysteine | Saccharomyces cerevisiae | - |
S-geranylgeranyl-protein + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate | 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, but 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 g-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families | Saccharomyces cerevisiae | |
geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate | 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 | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
geranylgeranyl diphosphate + protein-cysteine | - |
Saccharomyces cerevisiae | S-geranylgeranyl-protein + diphosphate | - |
? | |
geranylgeranyl diphosphate + protein-cysteine | prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits | Saccharomyces cerevisiae | S-geranylgeranyl-protein + diphosphate | - |
? | |
geranylgeranyl diphosphate + protein-cysteine | enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X. X is Leu or Phe | Saccharomyces cerevisiae | S-geranylgeranyl-protein + diphosphate | - |
? | |
geranylgeranyl diphosphate + protein-cysteine | enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X | Saccharomyces cerevisiae | S-geranylgeranyl-protein + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | alpha,beta, 1 * 48000 + 1 * 43000 | Saccharomyces cerevisiae |