Literature summary 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.

Application

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

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	Rattus norvegicus	-	S-farnesyl protein + diphosphate	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.5.1.58	Rattus norvegicus	-	-	-

Reaction

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

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Release 2023.1 (January 2023)