CHEBI:149638 - 5-methoxy-D-tryptophan zwitterion
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InChI=1S/C12H14N2O3/c1-17-8-2-3-11-9(5-8)7(6-14-11)4-10(13)12(15)16/h2-3,5-6,10,14H,4,13H2,1H3,(H,15,16)/t10-/m1/s1 |
KVNPSKDDJARYKK-SNVBAGLBSA-N |
O(C)C1=CC2=C(NC=C2C[C@@H]([NH3+])C(=O)[O-])C=C1 |
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5-methoxy-D-tryptophan
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UniProt
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Hai Y, Jenner M, Tang Y (2019) Complete Stereoinversion of l-Tryptophan by a Fungal Single-Module Nonribosomal Peptide Synthetase. Journal of the American Chemical Society 141, 16222-16226 (Source: SUBMITTER) [PubMed:31573806] [show Abstract] 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. Here, 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. |
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