The berberine bridge enzyme (BBE)-like flavoproteins have attracted continuous attention for their capability to catalyze various oxidative reactions. Here we demonstrate that MitR, a secreted BBE-like enzyme, functions as a special drug-binding efflux protein evolved from quinone reductase. Moreover, this protein provides self-resistance to its hosts toward the DNA-alkylating agent mitomycin C with a distinctive strategy, featured by independently performing drug binding and efflux.
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http://dx.doi.org/10.1021/acs.orglett.4c00042 | DOI Listing |
J Plant Res
January 2025
School of Geography and Environment, Liaocheng University, Liaocheng, Shandong, 252059, China.
Biochar and SiO NPs are effective soil conditioners, but the impacts and mechanisms of combined application in oilseed rape are not yet clear. Therefore, an experiment was designed to investigate oilseed rape growth, physiological indexes, and transcriptome sequencing under four treatments: control (CK), Platanus orientalis L. leaf biochar (B), SiO NPs (S), and BS.
View Article and Find Full Text PDFBiochemistry
September 2024
Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen 9747 AG, The Netherlands.
Berberine bridge enzyme-like oxidases are often involved in natural product biosynthesis and are seen as essential enzymes for the generation of intricate pharmacophores. These oxidases have the ability to transfer a hydride atom to the FAD cofactor, which enables complex substrate modifications and rearrangements including (intramolecular) cyclizations, carbon-carbon bond formations, and nucleophilic additions. Despite the diverse range of activities, the mechanistic details of these reactions often remain incompletely understood.
View Article and Find Full Text PDFOrg Lett
February 2024
School of Chemistry and Materials Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, China.
The berberine bridge enzyme (BBE)-like flavoproteins have attracted continuous attention for their capability to catalyze various oxidative reactions. Here we demonstrate that MitR, a secreted BBE-like enzyme, functions as a special drug-binding efflux protein evolved from quinone reductase. Moreover, this protein provides self-resistance to its hosts toward the DNA-alkylating agent mitomycin C with a distinctive strategy, featured by independently performing drug binding and efflux.
View Article and Find Full Text PDFPlant Physiol Biochem
January 2023
Department of Physical and Chemical Sciences, University of L'Aquila, L'Aquila, 67100, Italy. Electronic address:
Oligogalacturonides (OGs) are pectin fragments released from the breakdown of the homogalacturonan during pathogenesis that act as Damage-Associated Molecular Patterns. OG-oxidase 1 (OGOX1) is an Arabidopsis berberine bridge enzyme-like (BBE-l) oligosaccharide oxidase that oxidizes OGs, impairing their elicitor activity and concomitantly releasing HO. The OG-oxidizing activity of OGOX1 is markedly pH-dependent, with optimum pH around 10, and is higher towards OGs with a degree of polymerization higher than two.
View Article and Find Full Text PDFOrg Lett
August 2022
Institut für Pharmazeutische Biologie und Biotechnologie, Fachbereich Pharmazie, Philipps-Universität Marburg, Robert-Koch-Straße 4, 35037 Marburg, Germany.
Annullatins from are alkylated aromatic polyketides including annullatin D with a fused dihydrobenzofuran lactone ring system. Here, we report the identification of a silent biosynthetic gene cluster for annullatins from by heterologous expression in , gene deletion, and feeding experiments as well as by biochemical characterization. The polyketide core structure is consecutively modified by hydroxylation and prenylation.
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