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Literature summary extracted from

  • Casey, P.J.; Seabra, M.C.
    Protein prenyltransferases (1996), J. Biol. Chem., 271, 5289-5292.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.58 medicine evidence that inhibitors of enzyme could be effective therapeutic agents in treatment of many human cancers Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.58 Mg2+ required Saccharomyces cerevisiae
2.5.1.58 Zn2+ required Saccharomyces cerevisiae
2.5.1.59 Cd2+ the zinc in enzyme can be replaced by Cd2+ Saccharomyces cerevisiae
2.5.1.59 Mg2+ no requirement Saccharomyces cerevisiae
2.5.1.59 Zn2+ A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.58 46000
-
 alpha,beta, 1 * 48000 + 1 * 46000 Saccharomyces cerevisiae
2.5.1.58 48000
-
 alpha,beta, 1 * 48000 + 1 * 46000 Saccharomyces cerevisiae
2.5.1.59 43000
-
 alpha,beta, 1 * 48000 + 1 * 43000 Saccharomyces cerevisiae
2.5.1.59 48000
-
 alpha,beta, 1 * 48000 + 1 * 43000 Saccharomyces cerevisiae
2.5.1.60 38000
-
 alpha,beta, 1 * 60000 + 1 * 38000 Saccharomyces cerevisiae
2.5.1.60 60000
-
 alpha,beta, 1 * 60000 + 1 * 38000 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.58 farnesyl diphosphate + protein-cysteine Saccharomyces cerevisiae
-
 S-farnesyl protein + diphosphate
-
 ?
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine Saccharomyces cerevisiae
-
 S-geranylgeranyl-protein + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.58 Saccharomyces cerevisiae
-
-
-
2.5.1.59 Saccharomyces cerevisiae
-
-
-
2.5.1.60 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.58 farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate kinetic mechanism Saccharomyces cerevisiae
a
2.5.1.58 farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate enzyme constitutes the protein prenyltransferase family of enzymes Saccharomyces cerevisiae
a
2.5.1.58 farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate farnesyl diphosphate binds the enzyme in a two step process that may involve an enzyme conformational change, the enzyme-substrate complex then rapidly reacts with the peptide substrate to form a product, and product release is the rate-limiting step in catalysis Saccharomyces cerevisiae
a
2.5.1.59 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
a
2.5.1.59 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
a
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate enzyme is unique in the protein prenyltransferase family, consisting protein farnesyltransferase, EC 2.5.1.58, protein geranylgeranyltransferase type I, EC 2.5.1.59 and Rab geranylgeranyltransferase Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.58 farnesyl diphosphate + protein-cysteine prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F Saccharomyces cerevisiae diphosphate + S-farnesyl protein
-
 ?
2.5.1.58 farnesyl diphosphate + protein-cysteine
-
 Saccharomyces cerevisiae S-farnesyl protein + diphosphate
-
 ?
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine
-
 Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.59 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
-
 ?
2.5.1.59 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
-
 ?
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine enzyme 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 only if Rab is bound to a carrier protein termed Rab escort protein, REP Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine Rab protein forms a stable complex with Rab escort protein, REP Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.58 heterodimer alpha,beta, 1 * 48000 + 1 * 46000 Saccharomyces cerevisiae
2.5.1.59 heterodimer alpha,beta, 1 * 48000 + 1 * 43000 Saccharomyces cerevisiae
2.5.1.60 heterodimer alpha,beta, 1 * 60000 + 1 * 38000 Saccharomyces cerevisiae