Creating Flavin Reductase Variants with Thermostable and Solvent‐Tolerant Properties by Rational‐Design Engineering

• Published in: Chembiochem : a European journal of chemical biology Vol. 21; no. 10; pp. 1481 - 1491
• Main Authors: Maenpuen, Somchart, Pongsupasa, Vinutsada, Pensook, Wiranee, Anuwan, Piyanuch, Kraivisitkul, Napatsorn, Pinthong, Chatchadaporn, Phonbuppha, Jittima, Luanloet, Thikumporn, Wijma, Hein J., Fraaije, Marco W., Lawan, Narin, Chaiyen, Pimchai, Wongnate, Thanyaporn
• Format: Journal Article
• Language: English
• Published: Germany Wiley Subscription Services, Inc 15.05.2020
• Subjects: Acetic acid; biocatalysis; Chemical reactions; computational chemistry; Computer applications; Computer simulation; Design engineering; Flavin mononucleotide; Flavin reductase; flavoproteins; Heat treatment; Heat treatments; Hydrophobicity; Hydroxylase; Industrial applications; Molecular dynamics; Monooxygenase; Mutation; Reductases; Solvents; Temperature tolerance; Thermal stability; thermostable enzymes; computational chemistry; reductases; biocatalysis; flavoproteins; thermostable enzymes

We have employed computational approaches—FireProt and FRESCO—to predict thermostable variants of the reductase component (C1) of (4‐hydroxyphenyl)acetate 3‐hydroxylase. With the additional aid of experimental results, two C1 variants, A166L and A58P, were identified as thermotolerant enzymes, with...