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Literature summary for 2.5.1.59 extracted from

  • Zhang, F.L.; Casey, P.J.
    Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I (1996), Biochem. J., 320, 925-932.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
-
Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ the zinc in enzyme can be replaced by Cd2+ Rattus norvegicus
Cd2+ Cd-substituted enzyme has altered specificities with regard to utilization of both peptide and isoprenoid substrates Rattus norvegicus
Mg2+ no requirement Rattus norvegicus
Zn2+ A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
geranylgeranyl diphosphate + protein-cysteine Rattus norvegicus
-
S-geranylgeranyl-protein + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
geranylgeranyl diphosphate + protein-cysteine
-
Rattus norvegicus S-geranylgeranyl-protein + diphosphate
-
?