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J. Biol. Chem., Vol. 268, Issue 6, 4055-4060, 02, 1993
K Yokoyama and MH Gelb
A protein geranylgeranyltransferase (PGGT) that transfers the
geranylgeranyl group from geranylgeranyl pyrophosphate (GGPP) to the
cysteine residue in the C-terminal sequence Cys-Ali-Ali-Leu (Ali is an
aliphatic amino acid) of proteins and peptides has been purified to
apparent homogeneity from bovine brain. This was accomplished by affinity
chromatography of partially purified enzyme on a gel containing a
covalently attached hexapeptide SSCILL. This peptide was identified as a
tight-binding ligand of the PGGT by employing a semi- random peptide
synthetic strategy. The purified enzyme consists of two subunits of
apparent molecular mass 40 and 48 kDa. Affinity-purified PGGT effectively
catalyzes the prenylation of peptides that contain a C- terminal Leu or Phe
residue. The PGGT forms a stable binary complex with intact GGPP that can
be isolated by gel filtration. Addition of a peptide substrate to this
complex results in the quantitative transfer of the prenyl group to the
peptide. This transfer occurs without the equilibration of enzyme-bound
GGPP with free GGPP. When the PGGT was incubated with farnesyl
pyrophosphate, the amount of binary complex formed was about 25% of that
formed with GGPP.
Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex
Department of Chemistry, University of Washington, Seattle 98195.
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