Identification two key residues at the intersection of domains of a thioether monooxygenase for improving its sulfoxidation performance

• Published in: Biotechnology and bioengineering Vol. 118; no. 2; pp. 737 - 744
• Main Authors: Ren, Shi‐Miao, Liu, Feng, Wu, Yin‐Qi, Chen, Qi, Zhang, Zhi‐jun, Yu, Hui‐Lei, Xu, Jian‐He
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01.02.2021
• Subjects: (S)‐omeprazole; Binding; biocatalysis; Cyclohexanone; Cyclohexanone monooxygenase; Domains; Mutagenesis; Mutants; Mutation; Omeprazole; protein engineering; Residues; Substrate inhibition; Sulfides; Sulfoxidation; thioether monooxygenases; (S)-omeprazole; thioether monooxygenases; protein engineering; biocatalysis
• ISSN: 0006-3592; 1097-0290; 1097-0290
• DOI: 10.1002/bit.27604

AcCHMO, a cyclohexanone monooxygenase from Acinetobacter calcoaceticus, is a typical Type I Baeyer–Villiger monooxygenase (BVMO). We previously obtained the AcCHMOM6 mutant, which oxidizes omeprazole sulfide (OPS) to the chiral sulfoxide drug esomeprazole. To further improve the catalytic efficiency...