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Literature summary extracted from

  • Pylypenko, O.; Rak, A.; Reents, R.; Niculae, A.; Sidorovitch, V.; Cioaca, M.D.; Bessolitsyna, E.; Thoma, N.H.; Waldmann, H.; Schlichting, I.; Goody, R.S.; Alexandrov, K.
    Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase (2003), Mol. Cell, 11, 483-494.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.60 at 2.7 Angstom, crystal structure of REP-1 in complex with farnesyl-loaded enzyme, contact between the two proteins is formed through domain II of REP-1 and the alpha subunit of the enzyme Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.60 Rattus norvegicus
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Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.60 geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate mechanism of enzyme/REP-complex formation Rattus norvegicus
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

Substrates and Products (Substrate)

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