金黄色葡萄球菌中芳胺n -乙酰转移酶活性。

F C Chang, J G Chung, W C Chang, L T Wu, G W Chen, S H Chang
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引用次数: 0

摘要

采用对氨基苯甲酸(PABA)或2-氨基芴(2-AF)孵育金黄色葡萄球菌细胞质,采用高压液相色谱法测定n -乙酰转移酶(NAT)活性。结果表明,金黄色葡萄球菌对2-AF乙酰化的NAT活性为0.67 +/- 0.04 nmol/min/mg,对PABA乙酰化的NAT活性为0.46 +/- 0.02 nmol/min/mg。2-AF的表观K(m)和Vmax分别为2.85 +/- 0.65 mM和7.51 +/- 0.86 nmol/min/mg蛋白,PABA的表观K(m)和Vmax分别为2.35 +/- 0.39 mM和9.43 +/- 0.78 nmol/min/mg蛋白。两种底物酶活性的最佳pH值均为7.0。两种底物酶活性的最佳温度均为37℃。0.25 mM碘乙酰胺对NAT活性有抑制作用,活性降低50%。1.0 mM时,碘乙酰胺活性被抑制90%以上。在一系列二价阳离子和盐中,Zn2+、Ca2+和Fe2+被证明是最有效的抑制剂。从金黄色葡萄球菌中分离得到的NAT分子量为44.9 kDa。本文首次证实了乙酰辅酶a:芳胺在金黄色葡萄球菌中的NAT活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Arylamine N-acetyltransferase activity in Staphylococcus aureus.

N-Acetyltransferase (NAT) activities were determined by incubation of Staphylococcus aureus cytosols with p-aminobenzoic acid (PABA) or 2-aminofluorene (2-AF) followed by high pressure liquid chromatography assays. The NAT activities from S. aureus were found to be 0.67 +/- 0.04 nmol/min/mg protein for the acetylation of 2-AF and 0.46 +/- 0.02 nmol/min/mg protein for the acetylation of PABA. The apparent K(m) and Vmax values obtained were 2.85 +/- 0.65 mM and 7.51 +/- 0.86 nmol/min/mg protein for 2-AF, and 2.35 +/- 0.39 mM and 9.43 +/- 0.78 nmol/min/mg protein for PABA, respectively. The optimal pH value for the enzyme activity was 7.0 for both substrates tested. The optimal temperature for enzyme activity was 37 degrees C for both substrates. The NAT activity was inhibited by iodoacetamide at 0.25 mM, and activity was reduced 50%. At 1.0 mM iodoacetamide activity was inhibited more than 90%. Among a series of divalent cations and salts, Zn2+, Ca2+, and Fe2+ were demonstrated to be the most potent inhibitors. The molecular weight of NAT from S. aureus was found to be 44.9 kDa. This report is the first demonstration of acetyl CoA: arylamine NAT activity in S. aureus.

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