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Literature summary 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)

EC Number Cloned (Comment) Organism
2.5.1.59
-
 Rattus norvegicus

Metals/Ions

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

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 Rattus norvegicus
-
 S-geranylgeranyl-protein + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.59 Rattus norvegicus
-
-
-

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 Rattus norvegicus
a

Substrates and Products (Substrate)

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