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Literature summary extracted from

  • Stirtan, W.G.; Poulter, C.D.
    Yeast protein geranylgeranyltransferase type-I: steady-state kinetics and substrate binding (1997), Biochemistry, 36, 4552-4557.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.59 alpha-subunit encoded by RAM2 and beta-subunit encoded by CDC43 translationally coupled by overlapping the RAM-CDC43 stop-start codons and by locating a ribosome-binding site near the 3' end of RAM2, recombinant enzyme overproduced in Escherichia coli Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.59 1-phosphono-(E,E,E)-geranylgeraniol competitive to geranylgeranyl diphosphate, potent substrate inhibition to dansyl-Gly-Cys-Ile-Ile-Leu Saccharomyces cerevisiae
2.5.1.59 Cys-3-(aminomethyl)benzoic acid-Leu noncompetitive to geranylgeranyl diphosphate, competitive to dansyl-Gly-Cys-Ile-Ile-Leu Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.59 0.00094
-
geranylgeranyl diphosphate pH 7.5, 30°C Saccharomyces cerevisiae
2.5.1.59 0.0018
-
dansyl-Gly-Cys-Ile-Ile-Leu pH 7.5, 30°C Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine Saccharomyces cerevisiae
-
S-geranylgeranyl-protein + diphosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.59 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate an ordered binding mechanism for enzyme where geranylgeranyl diphosphate adds before peptide Saccharomyces cerevisiae
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 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.59 geranylgeranyl diphosphate + dansyl-Gly-Cys-Ile-Ile-Leu
-
Saccharomyces cerevisiae dansyl-Gly-(S-geranylgeranyl)-Cys-Ile-Ile-Leu + diphosphate
-
?
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine
-
Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
?
2.5.1.59 geranylgeranyl diphosphate + protein-cysteine prenylation, substrates are Rho, Rac, most trimeric G protein gamma subunits Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
?
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. X is Leu or Phe Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
?
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 Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.59 0.34
-
geranylgeranyl diphosphate
-
Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.5.1.59 additional information
-
additional information KI for varied concentrations of dansyl-Gly-Cys-Ile-Ile-Leu Saccharomyces cerevisiae
2.5.1.59 0.0002
-
1-phosphono-(E,E,E)-geranylgeraniol with respect to geranylgeranyl diphosphate Saccharomyces cerevisiae
2.5.1.59 0.078
-
Cys-3-(aminomethyl)benzoicacid-Leu with respect to dansyl-Gly-Cys-Ile-Ile-Leu Saccharomyces cerevisiae
2.5.1.59 0.14
-
Cys-3-(aminomethyl)benzoicacid-Leu with respect to geranylgeranyl diphosphate Saccharomyces cerevisiae