Synthesis of the biologically important dideuterium-labelled adenosine triphosphate analogue ApppI(d₂)

• Petri A. Turhanen

Beilstein J. Org. Chem. 2022, 18, 1466–1470, doi:10.3762/bjoc.18.153

• prevent protein isoprenylation by inhibiting farnesyl pyrophosphate synthase in the mevalonate pathway. This process leads to the formation of a series of compounds of which the structures have been reported elsewhere [10][11][12][13]. In 2006, Mönkkönen et al. have reported that the use of NBPs led to

Posttranslational isoprenylation of tryptophan in bacteria

• Masahiro Okada,
• Tomotoshi Sugita and
• Ikuro Abe

Beilstein J. Org. Chem. 2017, 13, 338–346, doi:10.3762/bjoc.13.37

• Masahiro Okada Tomotoshi Sugita Ikuro Abe Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan 10.3762/bjoc.13.37 Abstract Posttranslational isoprenylation is generally recognized as a universal modification of the cysteine residues in peptides and

• same scaffold as that of the ComX pheromones, but with the opposite stereochemistry. This review highlights the biosynthetic pathways and posttranslational isoprenylation of tryptophan. In particular, recent studies on peptide modifying enzymes are discussed. Keywords: Bacillus subtilis

• ; isoprenylation; post-translational modification; quorum sensing; tryptophan; Introduction Posttranslational modification is the chemical modification of proteins after their translation from mRNAs to the corresponding polypeptide chains synthesized by ribosomes. Since a posttranslational modification generates