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Literature summary for 2.5.1.58 extracted from

  • Lane, K.T.; Beese, L.S.
    Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I (2006), J. Lipid Res., 47, 681-699.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ABT-839
-
Homo sapiens
BMS-214662
-
Homo sapiens
L-778,123
-
Homo sapiens
R115777
-
Homo sapiens
SCH66336
-
Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, stabilizes the developing negative charge on the diphosphate as the bond breaks between the a-phosphate and the C1 atom of the farnesyl group Homo sapiens
Zn2+ contains one Zn2+ ion per dimer, required for catalysis and peptide binding Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
1 * 48000 + 1 * 46000 Homo sapiens
48000
-
1 * 48000 + 1 * 46000 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
farnesyl diphosphate + protein-cysteine
-
Homo sapiens diphosphate + S-farnesyl protein
-
ir

Subunits

Subunits Comment Organism
heterodimer 1 * 48000 + 1 * 46000 Homo sapiens

Synonyms

Synonyms Comment Organism
FTase
-
Homo sapiens