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Literature summary extracted from

  • Boutin, J.A.; Marande, W.; Goussard, M.; Loynel, A.; Canet, E.; Fauchere, J.L.
    Chromatographic assay and peptide substrate characterization of partially purified farnesyl- and geranylgeranyltransferases from rat brain cytosol (1998), Arch. Biochem. Biophys., 354, 83-94.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.59 medicine S-prenylated enzymes are interesting targets for noncytotoxic anticancer agents Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.59 additional information
-
 additional information comparison of Km of 18 hexapeptides as potential substrates of the farnesyltransferase and geranylgeranyl transferaseI, recognition of overlapping sequences by farnesyltransferase and geranylgeranyltransferaseI Rattus norvegicus
2.5.1.59 0.00002
-
 Arg-Arg-Cys-Val-Leu-Leu pH 7.6, 30°C Rattus norvegicus
2.5.1.59 0.00013
-
 Lys-Lys-Cys-Ile-Ile-Met pH 7.6, 30°C Rattus norvegicus
2.5.1.59 0.002
-
 Lys-Pro-Cys-Val-Val-Met pH 7.6, 30°C Rattus norvegicus
2.5.1.59 0.002
-
 Phe-Phe-Cys-Ala-Ile-Leu pH 7.6, 30°C Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.5.1.59 cytosol
-
 Rattus norvegicus 5829
-

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.59 partial Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
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 Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.59 brain
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.59 geranylgeranyl diphosphate + Arg-Arg-Cys-Val-Leu-Leu
-
 Rattus norvegicus diphosphate + Arg-Arg-S-geranylgeranyl-Cys-Val-Leu-Leu
-
 ?
2.5.1.59 geranylgeranyl diphosphate + Leu-Pro-Cys-Val-Val-Met
-
 Rattus norvegicus diphosphate + Leu-Pro-S-geranylgeranyl-Cys-Val-Val-Met
-
 ?
2.5.1.59 geranylgeranyl diphosphate + Lys-Lys-Cys-Ile-Ile-Met
-
 Rattus norvegicus diphosphate + Lys-Lys-S-geranylgeranyl-Cys-Ile-Ile-Met
-
 ?
2.5.1.59 geranylgeranyl diphosphate + Lys-Pro-Cys-Val-Val-Met
-
 Rattus norvegicus Lys-Pro-(S-geranylgeranyl)-Cys-Val-Val-Met + diphosphate
-
 ?
2.5.1.59 geranylgeranyl diphosphate + Phe-Phe-Cys-Ala-Ile-Leu
-
 Rattus norvegicus diphosphate + Phe-Phe-S-geranylgeranyl-Cys-Ala-Ile-Leu
-
 ?
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 Rattus norvegicus S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.59 additional information some of the 18 analysed hexapeptides effieciently farnsylated by enzyme Rattus norvegicus ?
-
 ?