Predicting the Substrate Scope of the Flavin‐Dependent Halogenase BrvH
Abstract: The recently described flavin‐dependent halogenase BrvH is able to catalyse both the bromination and chlorination of indole, but shows significantly higher bromination activity. BrvH was annotated as a tryptophan halogenase, but does not accept tryptophan as a substrate. Its native substrate remains unknown. A predictive model with the data available for BrvH was analysed. A training set of compounds tested in vitro was docked into the active site of a complete protein model based on the X‐ray structure of BrvH. The atoms not resolved experimentally were modelled by using molecular mechanics force fields to obtain this protein model. Furthermore, docking poses for the substrates and known non‐substrates have been calculated. Parameters like distance, partial charge and hybridization state were analysed to derive rules for predicting activity. With this model for activity of the BrvH, a virtual screening suggested several structures for potential substrates. Some of the compounds preselected in this way were tested in vitro, and several could be verified as convertible substrates. Based on information on halogenated natural products, a new dataset was created to specifically search for natural products as substrates/products, and virtual screening in this database yielded further hits.
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
Predicting the Substrate Scope of the Flavin‐Dependent Halogenase BrvH ; volume:21 ; number:22 ; year:2020 ; pages:3282-3288 ; extent:7
ChemBioChem ; 21, Heft 22 (2020), 3282-3288 (gesamt 7)
- Urheber
- DOI
-
10.1002/cbic.202000444
- URN
-
urn:nbn:de:101:1-2022062007194801722767
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:23 MESZ
Datenpartner
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Neubauer, Pia R.
- Pienkny, Silke
- Wessjohann, Ludger
- Brandt, Wolfgang
- Sewald, Norbert
Ähnliche Objekte (12)
Broadening the Scope of the Flavin‐Tag Method by Improving Flavin Incorporation and Incorporating Flavin Analogs
Expanding the scope of group E flavin monooxygenases : novel insights into the physiological and biotechnological role of these flavin dependent monooxygenases
Broadening The Substrate Scope of Aldolases Through Metagenomic Enzyme Discovery
Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
Exploring the Substrate Scope and Catalytic Promiscuity of Nitroreductase‐Like Enzymes
Enzyme evolution: exploring substrate scope and catalytic promiscuity
Broadening the scope of Pd-catalyzed oscillatory carbonylation reactions: solvent, substrate, catalyst
On the Substrate Scope of Dimethylsulfonium Propionate Lyases toward Dimethylsulfoxonium Propionate Derivatives
Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae
The structure of the covalent flavin adduct formed between lactate oxidase and the suicide substrate 2-hydroxy-3-butynoate
Influence of Substrate Binding Residues on the Substrate Scope and Regioselectivity of a Plant O‐Methyltransferase against Flavonoids
Scope for predicting seasonal variation of the SPCZ with ACCESS-S1
Broadening the Scope of the Flavin‐Tag Method by Improving Flavin Incorporation and Incorporating Flavin Analogs
Expanding the scope of group E flavin monooxygenases : novel insights into the physiological and biotechnological role of these flavin dependent monooxygenases
Broadening The Substrate Scope of Aldolases Through Metagenomic Enzyme Discovery
Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
Exploring the Substrate Scope and Catalytic Promiscuity of Nitroreductase‐Like Enzymes
Enzyme evolution: exploring substrate scope and catalytic promiscuity
Broadening the scope of Pd-catalyzed oscillatory carbonylation reactions: solvent, substrate, catalyst
On the Substrate Scope of Dimethylsulfonium Propionate Lyases toward Dimethylsulfoxonium Propionate Derivatives
Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae
The structure of the covalent flavin adduct formed between lactate oxidase and the suicide substrate 2-hydroxy-3-butynoate
Influence of Substrate Binding Residues on the Substrate Scope and Regioselectivity of a Plant O‐Methyltransferase against Flavonoids
Scope for predicting seasonal variation of the SPCZ with ACCESS-S1
Broadening the Scope of the Flavin‐Tag Method by Improving Flavin Incorporation and Incorporating Flavin Analogs
Expanding the scope of group E flavin monooxygenases : novel insights into the physiological and biotechnological role of these flavin dependent monooxygenases
Broadening The Substrate Scope of Aldolases Through Metagenomic Enzyme Discovery
Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
Exploring the Substrate Scope and Catalytic Promiscuity of Nitroreductase‐Like Enzymes
Enzyme evolution: exploring substrate scope and catalytic promiscuity
Broadening the scope of Pd-catalyzed oscillatory carbonylation reactions: solvent, substrate, catalyst
On the Substrate Scope of Dimethylsulfonium Propionate Lyases toward Dimethylsulfoxonium Propionate Derivatives
Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae
The structure of the covalent flavin adduct formed between lactate oxidase and the suicide substrate 2-hydroxy-3-butynoate
Influence of Substrate Binding Residues on the Substrate Scope and Regioselectivity of a Plant O‐Methyltransferase against Flavonoids