Dissecting the low catalytic capability of flavin-dependent halogenases.

Catalysis Crystallography, X-Ray Flavin-Adenine Dinucleotide / metabolism Flavins / metabolism Halogenation Hydrogen Peroxide / metabolism Kinetics Models, Molecular Oxidoreductases / metabolism Protein Conformation
QM/MM calculations X-ray structures flavin monooxygenase halogenase kinetics stopped-flow

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
Historique:
received: 10 09 2020
revised: 11 11 2020
accepted: 13 11 2020
pubmed: 20 1 2021
medline: 15 9 2021
entrez: 19 1 2021
Statut: ppublish

Résumé

Although flavin-dependent halogenases (FDHs) are attractive biocatalysts, their practical applications are limited because of their low catalytic efficiency. Here, we investigated the reaction mechanisms and structures of tryptophan 6-halogenase (Thal) from Streptomyces albogriseolus using stopped-flow, rapid-quench flow, quantum/mechanics molecular mechanics calculations, crystallography, and detection of intermediate (hypohalous acid [HOX]) liberation. We found that the key flavin intermediate, C4a-hydroperoxyflavin (C4aOOH-FAD), formed by Thal and other FDHs (tryptophan 7-halogenase [PrnA] and tryptophan 5-halogenase [PyrH]), can react with I

Identifiants

DOI: 10.1074/jbc.RA120.016004 PMID: 33465708 PMC: PMC7948982
pubmed: 33465708
pii: S0021-9258(20)00055-1
doi: 10.1074/jbc.RA120.016004
pmc: PMC7948982
pii:
doi:

Substances chimiques

Flavins 0
Flavin-Adenine Dinucleotide 146-14-5
Hydrogen Peroxide BBX060AN9V
Oxidoreductases EC 1.-
tryptophan halogenase EC 1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

100068

Subventions

Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L01386X/1
Pays : United Kingdom

Informations de copyright

Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflict of interest with the contents of this article.

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Auteurs

Aisaraphon Phintha (A)

Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok, Thailand; School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.

Kridsadakorn Prakinee (K)

School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.

Aritsara Jaruwat (A)

Biomolecular Analysis and Application Research Team, National Center for Genetic Engineering and Biotechnology, Klong Luang, Pathumthani, Thailand.

Narin Lawan (N)

Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.

Surawit Visitsatthawong (S)

School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.

Chadaporn Kantiwiriyawanitch (C)

School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.

Warangkhana Songsungthong (W)

Biomolecular Analysis and Application Research Team, National Center for Genetic Engineering and Biotechnology, Klong Luang, Pathumthani, Thailand.

Duangthip Trisrivirat (D)

School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand.

Pirom Chenprakhon (P)

Institute for Innovative Learning, Mahidol University, Nakhon Pathom, Thailand.

Adrian Mulholland (A)

Centre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol, UK.

Karl-Heinz van Pée (KH)

General Biochemistry, Faculty of Chemistry and Food Chemistry, Technical University of Dresden, Dresden, Germany.

Penchit Chitnumsub (P)

Biomolecular Analysis and Application Research Team, National Center for Genetic Engineering and Biotechnology, Klong Luang, Pathumthani, Thailand. Electronic address: penchit@biotec.or.th.

Pimchai Chaiyen (P)

Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok, Thailand; School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand. Electronic address: pimchai.chaiyen@vistec.ac.th.

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Classifications MeSH

questionsmedicales.fr › Phénomènes chimiques › Catalyse › Dissecting the low catalytic capability of...
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Cristallographie aux rayons X › Dissecting the low catalytic capability of...
questionsmedicales.fr › Facteurs biologiques › Pigments biologiques › Flavines › Riboflavine › Flavine adénine dinucléotide › Dissecting the low catalytic capability of...
questionsmedicales.fr › Facteurs biologiques › Pigments biologiques › Flavines › Dissecting the low catalytic capability of...
questionsmedicales.fr › Métabolisme › Halogénation › Dissecting the low catalytic capability of...
questionsmedicales.fr › Composés chimiques organiques › Radicaux libres › Peroxydes › Peroxyde d'hydrogène › Dissecting the low catalytic capability of...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Cinétique › Dissecting the low catalytic capability of...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Dissecting the low catalytic capability of...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Oxidoreductases › Dissecting the low catalytic capability of...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Dissecting the low catalytic capability of...