Abstract
Formula presented 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.
| Original language | English |
|---|---|
| Pages (from-to) | 815-817 |
| Number of pages | 3 |
| Journal | Organic Letters |
| Volume | 1 |
| Issue number | 5 |
| DOIs | |
| State | Published - 9 Sep 1999 |
Keywords
- Alkyl and Aryl Transferases/metabolism
- Alkylation
- Cysteine/metabolism
- Peptides/analysis
- Polyisoprenyl Phosphates
- Protein Binding
- Saccharomyces cerevisiae/enzymology
- Sesquiterpenes
- Spectrometry, Mass, Electrospray Ionization
- Thermodynamics
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