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

BRENDA support

Literature summary extracted from

  • Dursina, B.; Thomä, N.H.; Sidorovitch, V.; Niculae, A.; Iakovenko, A.; Rak, A.; Albert, S.; Ceacareanu, A.C.; Kolling, R.; Herrmann, C.; Goody, R.S.; Alexandrov, K.
    Interaction of yeast Rab geranylgeranyl transferase with its protein and lipid substrates (2002), Biochemistry, 41, 6805-6816.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.60 expression in Escherichia coli Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.60 additional information
-
 additional information yeast enzyme displays significantly lower affinity for its reaction product than its mammalian counterpart Rattus norvegicus
2.5.1.60 additional information
-
 additional information yeast enzyme displays significantly lower affinity for its reaction product than its mammalian counterpart Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine Rattus norvegicus reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine Saccharomyces cerevisiae reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins S-geranylgeranyl-protein + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.60 Rattus norvegicus
-
-
-
2.5.1.60 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate enzyme is unique in the protein prenyltransferase family, consisting protein farnesyltransferase, EC 2.5.1.58, protein geranylgeranyltransferase type I, EC 2.5.1.59 and Rab geranylgeranyltransferase Rattus norvegicus
a
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate enzyme is unique in the protein prenyltransferase family, consisting protein farnesyltransferase, EC 2.5.1.58, protein geranylgeranyltransferase type I, EC 2.5.1.59 and Rab geranylgeranyltransferase Saccharomyces cerevisiae
a
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate mammalian enzyme have revealed two alternative pathways for the assembly of catalytic complex. The classical pathway: the Rab protein forms a stable complex with REP. Enzyme covalently attaches the geranylgeranyl groups to two C-terminal cysteines of the Rab protein. Upon prenylation, the Rab/REP complex remains tightly associated with the enzyme until binding of a new molecule of isoprenoid decreases its affinity for the prenylated complex. The prenylated complex dissociated from enzyme and delivers Rab protein to its target membrane. In the alternative pathway, enzyme and REP form a tight complex in the presence of the phosphoisoprenoid. This complex is catalytically competent and can recruit and prenylate Rab protein. Rattus norvegicus
a
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate mammalian enzyme have revealed two alternative pathways for the assembly of catalytic complex. The classical pathway: the Rab protein forms a stable complex with REP. Enzyme covalently attaches the geranylgeranyl groups to two C-terminal cysteines of the Rab protein. Upon prenylation, the Rab/REP complex remains tightly associated with the enzyme until binding of a new molecule of isoprenoid decreases its affinity for the prenylated complex. The prenylated complex dissociated from enzyme and delivers Rab protein to its target membrane. In the alternative pathway, enzyme and REP form a tight complex in the presence of the phosphoisoprenoid. This complex is catalytically competent and can recruit and prenylate Rab protein. Saccharomyces cerevisiae
a
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate the yeast enzyme follows only the classical pathway Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine
-
 Rattus norvegicus S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine Rab protein forms a stable complex with Rab escort protein, REP Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins Rattus norvegicus S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins Saccharomyces cerevisiae S-geranylgeranyl-protein + diphosphate
-
 ?
2.5.1.60 additional information yeast enzyme binding of farnesyl diphosphate is as weaker as of geranylgeranyl diphosphate, the length of isoprenoids has an influence on their affinity for enzyme, but unlike the mammalian enzyme, yeast enzyme binds prenylated and unprenylated Yptp/Mrs6p complex with similar affinities, phosphoisoprenoids do not influence the affinity of Mrs6p for yeast enzyme Rattus norvegicus ?
-
 ?
2.5.1.60 additional information yeast enzyme binding of farnesyl diphosphate is as weaker as of geranylgeranyl diphosphate, the length of isoprenoids has an influence on their affinity for enzyme, but unlike the mammalian enzyme, yeast enzyme binds prenylated and unprenylated Yptp/Mrs6p complex with similar affinities, phosphoisoprenoids do not influence the affinity of Mrs6p for yeast enzyme Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.60 heterodimer alpha,beta, but structural differences between enzyme of higher and lower eukaryotes Rattus norvegicus
2.5.1.60 heterodimer alpha,beta, but structural differences between enzyme of higher and lower eukaryotes Saccharomyces cerevisiae
2.5.1.60 More yeast enzyme does not possess the immunoglobulin-like domain and a leucine-rich repeat domain found in mammalian enzyme Rattus norvegicus
2.5.1.60 More yeast enzyme does not possess the immunoglobulin-like domain and a leucine-rich repeat domain found in mammalian enzyme Saccharomyces cerevisiae