Yeast protein farnesyltransferase. Binding of S-alkyl peptides and related analogues.
[reaction: see text] Protein farnesyltransferase (PFTase) catalyzes alkylation of cysteine residues by farnesyl diphosphate (FPP). The dissociation constants for the PFTase-peptide analogue complexes for the series of analogues fl-RTRC(X)VIA (X = H, methyl, dodecyl, farnesyl) were measured by fluorescence anisotropy. The results indicate that an ionizable sulfhydryl moiety is important for substrate binding and the farnesyl group in the product facilitates binding.
Rozema
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DB
University of Utah, Department of Chemistry, 315 South 1400 East, Salt Lake City, Utah 84112, USA.
Phillips
S T
ST
Poulter
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CD
D019883:Alkyl and Aryl Transferases / Q000378:metabolism*; D000478:Alkylation; D003545:Cysteine / Q000378:metabolism; D010455:Peptides / Q000032:analysis*; D011106:Polyisoprenyl Phosphates; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012717:Sesquiterpenes; D021241:Spectrometry, Mass, Electrospray Ionization; D013816:Thermodynamics
D010455:Peptides; D011106:Polyisoprenyl Phosphates; D012717:Sesquiterpenes; C004808:farnesyl pyrophosphate; D019883:Alkyl and Aryl Transferases; C064911:p21(ras) farnesyl-protein transferase; D003545:Cysteine