Hyperthermophilic flavin reductase from Sulfolobus solfataricus P2: Production and biochemical characterization.
archaea
biodesulfurization
flavin reductase activity
hyperthermophile
oxidoreductase
Journal
Biotechnology and applied biochemistry
ISSN: 1470-8744
Titre abrégé: Biotechnol Appl Biochem
Pays: United States
ID NLM: 8609465
Informations de publication
Date de publication:
Nov 2019
Nov 2019
Historique:
received:
20
05
2019
accepted:
03
08
2019
pubmed:
10
8
2019
medline:
25
3
2020
entrez:
10
8
2019
Statut:
ppublish
Résumé
Nicotinamide adenine dinucleotide phosphate (NAD(P)H)-flavin oxidoreductases (flavin reductases) catalyze the reduction of flavin by NAD(P)H and provide the reduced form of flavin mononucleotide (FMN) to flavin-dependent monooxygenases. Based on bioinformatics analysis, we identified a putative flavin reductase gene, sso2055, in the genome of hyperthermophilic archaeon Sulfolobus solfataricus P2, and further cloned this target sequence into an expression vector. The cloned flavin reductase (EC. 1.5.1.30) was purified to homogeneity and characterized further. The purified enzyme exists as a monomer of 17.8 kDa, free of chromogenic cofactors. Homology modeling revealed this enzyme as a TIM barrel, which is also supported by circular dichroism measurements revealing a beta-sheet rich content. The optimal pH for SSO2055 activity was pH 6.5 in phosphate buffer and the highest activity observed was at 120 °C within the measurable temperature. We showed that this enzyme can use FMN and flavin adenine dinucleotide (FAD) as a substrate to generate their reduced forms. The purified enzyme is predicted to be a potential flavin reductase of flavin-dependent monooxygenases that could be involved in the biodesulfurization process of S. solfataricus P2.
Substances chimiques
Oxidoreductases
EC 1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
915-923Subventions
Organisme : Türkiye Bilimsel ve Teknolojik Araştirma Kurumu
ID : 110M001
Informations de copyright
© 2019 International Union of Biochemistry and Molecular Biology, Inc.
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