Dissecting the low catalytic capability of flavin-dependent halogenases

• Published in: The Journal of biological chemistry Vol. 296; p. 100068
• Main Authors: Phintha, Aisaraphon, Prakinee, Kridsadakorn, Jaruwat, Aritsara, Lawan, Narin, Visitsatthawong, Surawit, Kantiwiriyawanitch, Chadaporn, Songsungthong, Warangkhana, Trisrivirat, Duangthip, Chenprakhon, Pirom, Mulholland, Adrian, van Pée, Karl-Heinz, Chitnumsub, Penchit, Chaiyen, Pimchai
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.01.2021; American Society for Biochemistry and Molecular Biology
• Subjects: Catalysis; Crystallography, X-Ray; flavin monooxygenase; Flavin-Adenine Dinucleotide - metabolism; Flavins - metabolism; halogenase; Halogenation; Hydrogen Peroxide - metabolism; Kinetics; Models, Molecular; Oxidoreductases - metabolism; Protein Conformation; QM/MM calculations; stopped-flow; X-ray structures; halogenase; C1; Na2S2O4; flavin monooxygenase; PrnA; HOBr; QM/MM calculations; Thal; PyrH; HCOONa; X-ray structures; HPLC; FADH; HOI; DAD; MS; FAD; QM/MM; stopped-flow; HOX; NAD; HOCl; psFDH; DMSO-d6; kinetics

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-f...