78860-40-9Relevant academic research and scientific papers
METHODS FOR PRODUCING D-TRYPTOPHAN AND SUBSTITUTED D-TRYPTOPHANS
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Page/Page column 6; 10, (2021/04/01)
Single-module nonribosomal peptide synthetases (NRPSs) and NRPS-like enzymes activate and transform carboxylic acids in both primary and secondary metabolism; and are of great interest due to their biocatalytic potentials. The single-module NRPS IvoA is essential for fungal pigment biosynthesis. As disclosed herein, we show that IvoA catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a noncanonical C domain function. Using IvoA, we demonstrate a biocatalytic stereoinversion/deracemization route to access a variety of substituted D-tryptophan analogs in high enantiomeric excess.
METABOLIC PRODUCTS OF ASPERGILLUS TERREUS. V. DEMETHYLATION OF ASTERRIQUINONES
Arai, Kunizo,Shimizu, Sakae,Taguchi, Yasuhisa,Yamamoto, Yuzuru
, p. 991 - 999 (2007/10/02)
Demethylation of asterriquinones (AQ, bisindolyl-dimethoxyl benzoquinones) was investigated in connection with the determination of their structures and studies of their antitumor activity.Usually, the demethylation proceeded smoothly with KOH, but several types of side reactions were observed with acidic reagents.Keywords-demethylation; asterriquinones; Aspergillus terreus; IFO 8835; benzoquinone; indolyl; dimethylallyl
