ArticleNature communications2017
Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Advances in microbial biosynthesis of indirubin.Chinese herbal medicines · 2026Review
- Indigo production goes green: a review on opportunities and challenges of fermentative production.World journal of microbiology & biotechnology · 2024Review
- Late-Stage Chemoenzymatic Installation of Hydroxy-Bearing Allyl Moiety on the Indole Ring of Tryptophan-Containing Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Simplified quality assessment for small-molecule ligands in the Protein Data Bank.Structure (London, England : 1993) · 2022Article
- Efficient Bioproduction of Indigo and Indirubin by Optimizing a Novel Terpenoid Cyclase XiaI inACS omega · 2021Article
- Bacterial terpenome.Natural product reports · 2021Review
- Compartmentalization and Excretion of 2,4,6-Tribromophenol Sulfation and Glycosylation Conjugates in Rice Plants.Environmental science & technology · 2021Article
- Terpene synthases in disguise: enzymology, structure, and opportunities of non-canonical terpene synthases.Natural product reports · 2020Review
- Comparative genomics reveals a novel genetic organization of the sad cluster in the sulfonamide-degrader 'Candidatus Leucobacter sulfamidivorax' strain GP.BMC genomics · 2019Article
- Enzymatic Cascade Reactions in Biosynthesis.Angewandte Chemie (International ed. in English) · 2019Review
- Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities.Biology · 2018Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Terpenoid natural products comprise a wide range of molecular architectures that typically result from C-C bond formations catalysed by classical type I/II terpene cyclases. However, the molecular diversity of biologically active terpenoids is substantially increased by fully unrelated, non-canonical terpenoid cyclases. Their evolutionary origin has remained enigmatic. Here we report the in vitro reconstitution of an unusual flavin-dependent bacterial indoloterpenoid cyclase, XiaF, together with a designated flavoenzyme-reductase (XiaP) that mediates a key step in xiamycin biosynthesis. The crystal structure of XiaF with bound FADH
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.