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Beilstein J Org Chem

Title:		Posttranslational isoprenylation of tryptophan in bacteria
Author(s):		Okada M; Sugita T; Abe I;
Address:		"Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan"
Journal Title:		Beilstein J Org Chem
Year:		2017
Volume:		20170222
Issue:
Page Number:		338 - 346
DOI:		10.3762/bjoc.13.37
ISSN/ISBN:		1860-5397 (Print) 1860-5397 (Electronic) 1860-5397 (Linking)
Abstract:		"Posttranslational isoprenylation is generally recognized as a universal modification of the cysteine residues in peptides and the thiol groups of proteins in eukaryotes. In contrast, the Bacillus quorum sensing peptide pheromone, the ComX pheromone, possesses a posttranslationally modified tryptophan residue, and the tryptophan residue is isoprenylated with either a geranyl or farnesyl group at the gamma position to form a tricyclic skeleton that bears a newly formed pyrrolidine, similar to proline. The post-translational dimethylallylation of two tryptophan residues of a cyclic peptide, kawaguchipeptin A, from cyanobacteria has also been reported. Interestingly, the modified tryptophan residues of kawaguchipeptin A have the 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;
Notes:		"PubMed-not-MEDLINEOkada, Masahiro Sugita, Tomotoshi Abe, Ikuro eng Review Germany 2017/03/23 Beilstein J Org Chem. 2017 Feb 22; 13:338-346. doi: 10.3762/bjoc.13.37. eCollection 2017"