PURIFICATION AND PROPERTIES OF METHYL MERCAPTAN OXIDASE FROM THIOBACILLUS-THIOPARUS TK-M
PURIFICATION AND PROPERTIES OF METHYL MERCAPTAN OXIDASE FROM THIOBACILLUS-THIOPARUS TK-M
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DOI：
10.1099/00221287-138-1-217
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发表时间：
1992-01-01
期刊：
影响因子：
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通讯作者：
KANAGAWA, T
中科院分区：
文献类型：
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作者：
GOULD, WD;KANAGAWA, T
从生长在二甲硫醚上的硫杆菌 TK-m 中将甲硫醇 (MM)-氧化酶纯化至接近均质。该酶是一种 M(r) 值约为 40000 的单体。它按化学计量将 MM 氧化为甲醛、S2- 和 H2O2。该酶对于 MM 的 K(m) 为 31.3-mu-M。它还被证明可以氧化乙硫醇。 T. thioparus 的 MM-氧化酶与 Hyphomicrobium EG 的 MM-氧化酶具有一些不同的特征，例如较高的 K(m)、不被 S2- 抑制以及不能催化 S2- 的氧化。
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-mu-M 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-.