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Updated: Jan 22, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Pyrroloindoline cyclization in tryptophan-containing cyclodipeptides mediated by an unprecedented indole C3
Hongxia Li1, Yan Qiu1, Canxiong Guo1
1College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China. zhenggj@mail.buct.edu.cn zhusz@mail.buct.edu.cn.
Abstract:
Diverse bioactive alkaloids with a tryptophan 2,5-diketopiperazine (DKP) core and an annulated structure forming a methylated pyrroloindoline-DKP assembly have been isolated from various microbial sources. However, little is known about their biosynthesis. In this study, a novel indole C3 methyltransferase from Streptomyces sp. HPH0547 was discovered and characterized. Structural elucidation of the products revealed that this enzyme catalyzed unique pyrroloindoline cyclization in tryptophan-containing cyclodipeptides. This is the first C3 methyltransferase reported to catalyze pyrroloindoline cyclization in cyclic dipeptides, which provides a feasible and simple method to access diverse alkaloids.
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