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Literature summary for 2.5.1.58 extracted from

  • Casey, P.J.; Seabra, M.C.
    Protein prenyltransferases (1996), J. Biol. Chem., 271, 5289-5292.
    View publication on PubMed
Search for more literature for 2.5.1.58

Application

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae
Zn2+ required Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
 alpha,beta, 1 * 48000 + 1 * 46000 Saccharomyces cerevisiae
48000
-
 alpha,beta, 1 * 48000 + 1 * 46000 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate kinetic mechanism Saccharomyces cerevisiae
a
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate enzyme constitutes the protein prenyltransferase family of enzymes Saccharomyces cerevisiae
a
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
farnesyl diphosphate + protein-cysteine
-
 Saccharomyces cerevisiae S-farnesyl protein + diphosphate
-
 ?

Subunits

Subunits Comment Organism
heterodimer alpha,beta, 1 * 48000 + 1 * 46000 Saccharomyces cerevisiae