geranyl-pyrophosphate and farnesylacetic-acid

geranyl-pyrophosphate has been researched along with farnesylacetic-acid* in 1 studies

Other Studies

1 other study(ies) available for geranyl-pyrophosphate and farnesylacetic-acid

Article	Year
The geranyl-modified tryptophan residue is crucial for ComXRO-E-2 pheromone biological activity. Bioorganic & medicinal chemistry letters, 2011, Jul-01, Volume: 21, Issue:13 The ComX pheromone is an isoprenoidal oligopeptide containing a modified tryptophan residue, which stimulates natural genetic competence in gram-positive bacteria, Bacillus. We have reported the structure of the ComX(RO-E-2) pheromone, which is produced by the RO-E-2 strain of Bacillus subtilis. ComX(RO-E-2) analogs with substituted amino acids and isoprenoid modified tryptophan residues (e.g., prenyl, geranyl, and farnesyl), were synthesized and examined for biological activity. These results indicate that Phe-Trp(∗)(Ger)-NH(2) is the minimum pharmacophore of the ComX(RO-E-2) pheromone. Furthermore, the length of the isoprenoid moiety (i.e., modification style), and the presence of double bonds, are crucial for biological activity. The modification style of the ComX pheromone is more important than the peptide sequence with respect to biological activity. Topics: Amino Acid Sequence; Bacillus subtilis; Diphosphates; Diterpenes; Farnesol; Molecular Sequence Data; Molecular Structure; Neoprene; Pheromones; Tryptophan	2011

Article

Year

The geranyl-modified tryptophan residue is crucial for ComXRO-E-2 pheromone biological activity.

Bioorganic & medicinal chemistry letters, 2011, Jul-01, Volume: 21, Issue:13

The ComX pheromone is an isoprenoidal oligopeptide containing a modified tryptophan residue, which stimulates natural genetic competence in gram-positive bacteria, Bacillus. We have reported the structure of the ComX(RO-E-2) pheromone, which is produced by the RO-E-2 strain of Bacillus subtilis. ComX(RO-E-2) analogs with substituted amino acids and isoprenoid modified tryptophan residues (e.g., prenyl, geranyl, and farnesyl), were synthesized and examined for biological activity. These results indicate that Phe-Trp(∗)(Ger)-NH(2) is the minimum pharmacophore of the ComX(RO-E-2) pheromone. Furthermore, the length of the isoprenoid moiety (i.e., modification style), and the presence of double bonds, are crucial for biological activity. The modification style of the ComX pheromone is more important than the peptide sequence with respect to biological activity.

Topics: Amino Acid Sequence; Bacillus subtilis; Diphosphates; Diterpenes; Farnesol; Molecular Sequence Data; Molecular Structure; Neoprene; Pheromones; Tryptophan

2011