@article{mbs:/content/journal/micro/10.1099/00221287-138-1-217, author = "Gould, W. D. and Kanagawa, T.", title = "Purification and properties of methyl mercaptan oxidase from Thiobacillus thioparus TK-m", journal= "Microbiology", year = "1992", volume = "138", number = "1", pages = "217-221", doi = "https://doi.org/10.1099/00221287-138-1-217", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-138-1-217", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Summary: Methyl mercaptan (MM)-oxidase was purified to near homogeneity from Thiobacillus thioparus TK-m grown on dimethyl sulphide. The enzyme was a monomer with an M r value of approximately 40000. It oxidized MM stoichiometrically to formaldehyde, S2- and H2O2. The enzyme had a K m of 31·3 μM for MM. It was also shown to oxidize ethyl mercaptan. MM-oxidase from T. thioparus was shown to have some different characteristics from MM-oxidase of Hyphomicrobium EG, such as a higher K m, the absence of inhibition by S2- and the inability to catalyse the oxidation of S2-.", }