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首页> 外文期刊>Journal of bacteriology >Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium.
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Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium.

机译:鼠伤寒沙门氏菌S-硫代半胱氨酸合酶和半胱氨酸合酶B身份的酶促证明。

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S-Sulfocysteine synthase was isolated from Salmonella typhimurium LT-2 to homogeneous form with polyacrylamide gel electrophoresis. The molecular weight of this enzyme was determined to be ca. 55,000. The enzyme consisted of two identically sized subunits, and it contained one pyridoxal phosphate per subunit. The enzyme catalyzed the biosynthesis of cysteine or S-methylcysteine from sulfide or methanethiol and O-acetylserine, respectively, in addition to the formation of S-sulfocysteine from thiosulfate and O-acetylserine. The enzyme is identical to cysteine synthase B. The intracellular level of this enzyme was regulated by lesser extents of the same factors as those effective for cysteine synthase A.
机译:用聚丙烯酰胺凝胶电泳从鼠伤寒沙门氏菌LT-2中分离出S-磺基半胱氨酸合酶。该酶的分子量确定为约。 55,000。该酶由两个大小相同的亚基组成,每个亚基含有一个吡pyr醛磷酸酯。该酶除了由硫代硫酸盐和O-乙酰基丝氨酸形成S-磺基半胱氨酸之外,还分别催化了由硫化物或甲硫醇和O-乙酰基丝氨酸半胱氨酸或S-甲基半胱氨酸的生物合成。该酶与半胱氨酸合酶B相同。该酶的细胞内水平受与对半胱氨酸合酶A有效的因子相同程度的较小调节。

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