从大鼠肝脏中纯化一种催化酚类硫酸化反应的酶。
Purification from rat liver of an enzyme that catalyses the sulphurylation of phenols.
作者信息
McEvoy F A, Carroll J
出版信息
Biochem J. 1971 Aug;123(5):901-6. doi: 10.1042/bj1230901.
Abstract
- An enzyme (EC 2.8.2.1) that catalyses the transfer of sulphate from adenosine 3'-phosphate 5'-sulphatophosphate to phenols was purified approx. 2000-fold from male rat livers. 2. The purified preparation did not catalyse the sulphurylation of dehydroepiandrosterone, butan-1-ol, l-tyrosine methyl ester, 1-naphthylamine or serotonin. 3. At pH8.0 and 37 degrees C the K(m) values of the enzyme for p-nitrophenol and adenosine 3'-phosphate 5'-sulphatophosphate are 51 and 14mum respectively. The K(m) value for either substrate is independent of the concentration of the other. 4. The sulphurylation of phenol is inhibited by thiol compounds and glutathione at a concentration of 3mm caused an approx. 50% decrease in enzyme activity. 5. The K(m) of the enzyme for adenosine 3'-phosphate 5'-sulphatophosphate is unaffected by the presence of added glutathione but at a concentration of 5mm-glutathione the K(m) of the enzyme for its phenolic substrate is decreased.
摘要
- 一种催化硫酸从3'-磷酸腺苷5'-磷酸硫酸转移至酚类的酶（EC 2.8.2.1）从雄性大鼠肝脏中纯化得到，纯化倍数约为2000倍。2. 纯化后的制剂不催化脱氢表雄酮、丁醇、L-酪氨酸甲酯、1-萘胺或5-羟色胺的硫酸化反应。3. 在pH8.0和37℃条件下，该酶对对硝基苯酚和3'-磷酸腺苷5'-磷酸硫酸的K(m)值分别为51和14μmol/L。任一底物的K(m)值均与另一底物的浓度无关。4. 酚类的硫酸化反应受到硫醇化合物的抑制，3mmol/L的谷胱甘肽可使酶活性降低约50%。5. 3'-磷酸腺苷5'-磷酸硫酸的存在不影响该酶对其的K(m)值，但5mmol/L的谷胱甘肽会使该酶对酚类底物的K(m)值降低。
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