SUMMARY: Methyl mercaptan (MM)-oxidase was purified tenfold to near homogeneity from EG grown on dimethyl sulphoxide. The enzyme was a monomer with an value of about 40000-50000. It catalysed the formation of stoicheiometric amounts of formaldehyde, sulphide and HO from MM and O. It had a of 5-10 μ for MM and was strongly inhibited by substrate concentrations above 14 μ, the for this inhibition being 42 μ. Ethyl mercaptan and sulphide also served as substrates for the enzyme ( 18 and 60 μ respectively), whereas methanol was not oxidized. Upon oxidation of these compounds HO was formed. Although sulphide was a substrate for the enzyme, it also acted as a non-competitive inhibitor of MM oxidation ( 90 μ). Alcohol oxidase (EC purified from was also found to oxidize MM ( 110 μ) although at a low rate. The products formed were the same as for MM oxidation by the bacterial enzyme. In contrast to MM-oxidase however, alcohol oxidase was inactive with sulphide and was not inhibited by methyl mercaptan concentrations up to 500 μ.


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