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Literature summary extracted from

  • Buckner, F.S.; Eastman, R.T.; Nepomuceno-Silva, J.L.; Speelmon, E.C.; Myler, P.J.; Van Voorhis, W.C.; Yokoyama, K.
    Cloning, heterologous expression, and substrate specificities of protein farnesyltransferases from Trypanosoma cruzi and Leishmania major (2002), Mol. Biochem. Parasitol., 122, 181-188.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.58 medicine
-
 Trypanosoma cruzi
2.5.1.58 medicine enzyme from trypanosomatid parasites are target of anti-trypanosomatid agents because inhibitors of this enzyme are highly toxic to these parasites compared to mammalian cells Leishmania amazonensis
2.5.1.58 medicine enzyme from trypanosomatid parasites are target of anti-trypanosomatid agents because inhibitors of this enzyme are highly toxic to these parasites compared to mammalian cells Trypanosoma cruzi
2.5.1.58 medicine enzyme from trypanosomatid parasites are target of anti-trypanosomatid agents because inhibitors of this enzyme are highly toxic to these parasites compared to mammalian cells Leishmania major

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.58 coexpression of alpha and beta subunits of enzyme by Sf9 cells infected with a recombinant baculovirus Trypanosoma brucei brucei
2.5.1.58 coexpression of alpha and beta subunits of enzyme by Sf9 cells infected with a recombinant baculovirus Trypanosoma cruzi
2.5.1.58 coexpression of alpha and beta subunits of enzyme by Sf9 cells infected with a recombinant baculovirus Leishmania major

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.58 Zn2+ zinc ion is coordinated by three residues in the beta subunit: Asp-297, Cys-299, and H-362 and a water molecule Trypanosoma brucei brucei
2.5.1.58 Zn2+ zinc ion is coordinated by three residues in the beta subunit: Asp-297, Cys-299, and H-362 and a water molecule Trypanosoma cruzi
2.5.1.58 Zn2+ zinc ion is coordinated by three residues in the beta subunit: Asp-297, Cys-299, and H-362 and a water molecule Leishmania major

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.58 Leishmania amazonensis
-
-
-
2.5.1.58 Leishmania amazonensis LV78
-
-
-
2.5.1.58 Leishmania major Q8WR00 beta-subunit
-
2.5.1.58 Leishmania major Q8WR01 alpha-subunit
-
2.5.1.58 Trypanosoma brucei brucei
-
-
-
2.5.1.58 Trypanosoma cruzi Q8WR02 Tulahuen, beta-subunit
-
2.5.1.58 Trypanosoma cruzi Q8WR03 Tulahuen, allelic form II of the alpha-subunit
-
2.5.1.58 Trypanosoma cruzi Q8WR04 Tulahuen, allelic form I of the alpha-subunit
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.58 amastigote
-
 Leishmania major
-
2.5.1.58 epimastigote
-
 Trypanosoma cruzi
-
2.5.1.58 procyclic form
-
 Trypanosoma brucei brucei
-
2.5.1.58 promastigote
-
 Leishmania major
-
2.5.1.58 trypomastigote
-
 Trypanosoma cruzi
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.58 farnesyl diphosphate + protein-cysteine
-
 Leishmania amazonensis diphosphate + S-farnesyl protein
-
 ?
2.5.1.58 farnesyl diphosphate + protein-cysteine enzyme prefers Gln and Met at the X position but not Ser, Thr or Cys, which are good substrates for mammalian enzyme Trypanosoma brucei brucei diphosphate + S-farnesyl protein
-
 ?
2.5.1.58 farnesyl diphosphate + protein-cysteine enzyme prefers Gln and Met at the X position but not Ser, Thr or Cys, which are good substrates for mammalian enzyme Trypanosoma cruzi diphosphate + S-farnesyl protein
-
 ?
2.5.1.58 farnesyl diphosphate + protein-cysteine enzyme prefers Gln and Met at the X position but not Ser, Thr or Cys, which are good substrates for mammalian enzyme Leishmania major diphosphate + S-farnesyl protein
-
 ?
2.5.1.58 farnesyl diphosphate + protein-cysteine
-
 Leishmania amazonensis LV78 diphosphate + S-farnesyl protein
-
 ?