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Literature summary for 2.5.1.60 extracted from

  • Thomä, N.H.; Iakovenko, A.; Kalinin, A.; Waldmann, H.; Goody, R.S.; Alexandrov, K.
    Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II (2001), Biochemistry, 40, 268-274.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in SF21 cells 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 this posttranslational modification is essential for the biological activity of Rab proteins S-geranylgeranyl-protein + diphosphate
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?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Reaction

Reaction Comment Organism Reaction ID
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
geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate mechanism, geranylgeranyl diphosphate first acts as an allosteric regulator of enzyme, second acts as the phosphoisoprenoid donor in the prenylation reaction and third senses the completion of catalysis and concomitantly triggers substrate release by increasing the dissociation rate of the product Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
geranylgeranyl diphosphate + protein-cysteine
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Rattus norvegicus S-geranylgeranyl-protein + diphosphate
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?
geranylgeranyl diphosphate + protein-cysteine this posttranslational modification is essential for the biological activity of Rab proteins Rattus norvegicus S-geranylgeranyl-protein + diphosphate
-
?