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Literature summary for 2.5.1.58 extracted from

  • Furfine, E.S; Leban, J.J.; Landavazo, A.; Moomaw, J.F.; Casey, P.J.
    Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release (1995), Biochemistry, 34, 6857-6862.
    View publication on PubMed
Search for more literature for 2.5.1.58

Application

Application Comment Organism
medicine prime target for development of anticancer therapeutics Rattus norvegicus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate kinetic mechanism Rattus norvegicus
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 Rattus norvegicus
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 Rattus norvegicus diphosphate + S-farnesyl protein
-
 ir
farnesyl diphosphate + protein-cysteine
-
 Rattus norvegicus S-farnesyl protein + diphosphate
-
 ?