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Literature summary for 2.5.1.59 extracted from

  • Arellano, M.; Coll, P.M.; Yang, W.; Duran, A.; Tamanol, F.; Perez, P.
    Characterization of the geranylgeranyl transferase type I from Schizosaccharomyces pombe (1998), Mol. Microbiol., 29, 1357-1367.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
identification of the cwp1+ gene, which encodes the alpha-subunit of enzyme, coexpression of cwp1p and cwg2p, beta-subunit, in Escherichia coli Schizosaccharomyces pombe

Protein Variants

Protein Variants Comment Organism
additional information Cwg2-1 mutant has a defect in the actin organization, this mutant is identified as a single nucleotide change causing an A202T substitution in a residue conserved among the beta-subunit of enzyme, the deletion of cwg2 causes cell death Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
geranylgeranyl diphosphate + protein-cysteine Schizosaccharomyces pombe this prenylation is necessary for many proteins to interact with membrane localized at proper intracellular sites S-geranylgeranyl-protein + diphosphate
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?

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe
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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 Schizosaccharomyces pombe

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
geranylgeranyl diphosphate + protein-cysteine enzyme requires that protein substrates contain a Cys residue fourth from the C terminus, protein substrate motif: Cys-aliphatic-aliphatic-X Schizosaccharomyces pombe S-geranylgeranyl-protein + diphosphate
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?
geranylgeranyl diphosphate + protein-cysteine this prenylation is necessary for many proteins to interact with membrane localized at proper intracellular sites Schizosaccharomyces pombe S-geranylgeranyl-protein + diphosphate
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?
additional information requires geranylgeranylation of rho1p for the correct function of enzyme Schizosaccharomyces pombe ?
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?