20880-68-6Relevant articles and documents
Substrate promiscuity of the cyclic dipeptide prenyltransferases from Aspergillus fumigatus
Zou, Huixi,Zheng, Xiaodong,Li, Shu-Ming
, p. 44 - 52 (2009)
This study reports that a series of tryptophan derivatives with modifications on the side chain or at the indole ring were accepted by two cyclic dipeptide prenyltransferases, CdpNPT and FtmPT1, and converted to prenylated derivatives. The structures of t
Short, enantioselective total synthesis of okaramine N
Baran, Phil S.,Guerrero, Carlos A.,Corey
, p. 5628 - 5629 (2003)
The first enantioselective total synthesis of a member of the okaramine family of bis-indole alkaloids, okaramine N (1), has been accomplished via intermediates 2-7, as outlined. The N-prenylated derivative of (S)-tryptophan methyl ester (2) was coupled with Fmoc-protected N-tert-prenylated tryptophan (3) to form the amide 4 in 70% yield. Pd(II)-mediated cyclization/rearrangement, a key step in the synthesis, transformed 4 into the indoloazacine 5 (44%), which was deprotected and cyclized in a single step to give the hexacyclic diketopiperazine 6 (95%). In the following novel and key sequence, 6 was transformed into 1: (1) selective ene reaction with N-methyltriazolinedione, (2) photooxidation of the remaining tert-prenylated indole subunit to provide 7, and (3) thermal retroene reaction of 7 to afford okaramine N (70% from 6). Copyright
Functional characterization of the cyclomarin/cyclomarazine prenyltransferase cymd directs the biosynthesis of unnatural cyclic peptides
Schultz, Andrew W.,Lewis, Chad A.,Luzung, Michael R.,Baran, Phil S.,Moore, Bradley S.
, p. 373 - 377 (2010)
In vitro and in vivo characterization of the cyclomarin/cyclomarazine prenyltransferase CymD revea].ed its ability to prenylate tryptophan prior to incorporation into both cyclic peptides by the nonribosomal peptide synthetase CymA. This knowledge was utilized to bioengineer novel derivatives of these marine bacterial, natural products by providing synthetic N-alkyl tryptophans to a prenyltransferase-deficient mutant of Salinispora arenicola CNS-205.
