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Literature summary extracted from

  • Stirtan, W.G.; Poulter, C.D.
    Yeast protein geranylgeranyltransferase type-I: overproduction, purification, and characterization (1995), Arch. Biochem. Biophys., 321, 182-190.
    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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.59 0.001
-
 geranylgeranyl diphosphate pH 7.5, 30°C Saccharomyces cerevisiae
2.5.1.59 0.0024
-
 dansyl-Gly-Cys-Ile-Ile-Leu pH 7.5, 30°C Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.59 Mg2+ requirement, optimal activity at 0.5 mM in presence of 0.1 mM Zn2+ Saccharomyces cerevisiae
2.5.1.59 Zn2+ requirement, optimal activity of EDTA-treated enzyme at 0.01 mM in presence of 1 mM Mg2+ Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.59 34000
-
 alpha,beta, 1 * 34000 + 1 * 42000 Saccharomyces cerevisiae
2.5.1.59 42000
-
 alpha,beta, 1 * 34000 + 1 * 42000 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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.59 recombinant enzyme Saccharomyces cerevisiae

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 Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.59 geranylgeranyl diphosphate + dansyl-Cys-Ile-Ile-Leu
-
 Saccharomyces cerevisiae diphosphate + dansyl-S-geranylgeranyl-Cys-Ile-Ile-Leu
-
 ?
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 enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-Leu 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 Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.59 heterodimer alpha,beta, 1 * 34000 + 1 * 42000 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.59 7.5
-
-
 Saccharomyces cerevisiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.5.1.59 7 8.5
-
 Saccharomyces cerevisiae