A flavin-containing monooxygenase from <i>Schizosaccharomyces pombe</i>: characterization and application in the synthesis of <i>S</i>-methyl-L-cysteine sulfoxide.

Mengka LIAN; Zhaolin SONG; Wenjing GAO; Gang ZHU; Mengjun DONG; Yu LI; Yihan LIU; Fenghua WANG; Fuping LU

Return

A flavin-containing monooxygenase from Schizosaccharomyces pombe: characterization and application in the synthesis of S-methyl-L-cysteine sulfoxide.

Author: Mengka LIAN ¹ ; Zhaolin SONG ¹ ; Wenjing GAO ¹ ; Gang ZHU ¹ ; Mengjun DONG ¹ ; Yu LI ¹ ; Yihan LIU ¹ ; Fenghua WANG ¹ ; Fuping LU ¹
Author Information

1. Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, College of Bioengineering, Tianjin University of Science & Technology, Tianjin 300457, China.
Publication Type:Journal Article
Keywords: S-methyl-L-cysteine; S-methyl-L-cysteine sulfoxide; enzymatic properties; flavin-containing monooxygenase; metal ions
MeSH: Schizosaccharomyces/genetics*; Escherichia coli/metabolism*; Recombinant Proteins/metabolism*; Cysteine/biosynthesis*; Mixed Function Oxygenases/metabolism*; Schizosaccharomyces pombe Proteins/metabolism*; Oxygenases/metabolism*; Kinetics
From: Chinese Journal of Biotechnology 2025;41(1):474-485
CountryChina
Language:Chinese
Abstract: S-methyl-L-cysteine sulfoxide (SMCO) is a non-protein sulfur-containing amino acid with a variety of functions. There are few reports on the enzymes catalyzing the biosynthesis of SMCO from S-methyl-L-cysteine (SMC). In this study, the flavin-containing monooxygenase gene derived from Schizosaccharomyces pombe (spfmo) was heterologously expressed in Escherichia coli BL21(DE3) and the enzymatic properties of the expressed protein were analyzed. The optimum catalytic conditions of the recombinant SpFMO were 30 ℃ and pH 8.0, under which the enzyme activity reached 72.77 U/g. An appropriate amount of Mg²⁺ improved the enzyme activity. The enzyme kinetic analysis showed that the K_m and k_cat/K_m of SpFMO on the substrate SMC were 23.89 μmol/L and 61.71 L/(min·mmol), respectively. Under the optimal reaction conditions, the yield of SMCO synthesized from SMC catalyzed by SpFMO was 12.31% within 9 h. This study provides reference for the enzymatic synthesis of SMCO.