Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Saderholm, M.J.; Hightower, K.E.; Fierke, C.A.
    Role of metals in the reaction catalyzed by protein farnesyltransferase (2000), Biochemistry, 39, 12398-12405.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.58 medicine
-
Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.58 Mg2+ the magnesium affinity of enzyme increases with pH with a pka of 7.4, presumably reflecting the deprotonation of the farnesyl diphosphate to enhance magnesium coordination Rattus norvegicus
2.5.1.58 Mg2+ appears to coordinate the diphosphate moiety of farnesyl diphosphate Rattus norvegicus
2.5.1.58 additional information a metal-assisted nucleophile is involved in the catalytic mechanism of enzyme Rattus norvegicus
2.5.1.58 Zn2+ required Rattus norvegicus
2.5.1.58 Zn2+ zinc metalloenzyme 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 process necessary for the subcellular localisation of substrate to the plasma membrane 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

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
-
?
2.5.1.58 farnesyl diphosphate + protein-cysteine process necessary for the subcellular localisation of substrate to the plasma membrane Rattus norvegicus S-farnesyl protein + diphosphate
-
?
2.5.1.58 farnesyl monophosphate + Gly-Cys-Val-Leu-Ser
-
Rattus norvegicus phosphate + Gly-S-farnesyl-Cys-Val-Leu-Ser
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.58 additional information
-
additional information
-
Rattus norvegicus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.5.1.58 additional information
-
pH-dependence of the chemical step of product formation: the reaction is characterized by two ionizations, drastic differences in the pH dependence of farnesyl diphophate and farnesyl monophosphate, the magnesium affinity of enzyme increases with pH with a pka of 7.4 Rattus norvegicus