Corynebacterium glutamicum superoxide dismutase is a manganese-strict non-cambialistic enzyme in vitro
Corynebacterium glutamicum superoxide dismutase is a manganese-strict non-cambialistic enzyme in vitro
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DOI：
10.1016/j.micres.2006.05.005
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发表时间：
2008-01-01
影响因子：
6.7
通讯作者：
Guyonvarch, A.
中科院分区：
文献类型：
--
作者：
El Shafey, H. M.;Ghanem, S.;Guyonvarch, A.
对谷氨酸棒杆菌超氧化物歧化酶（SOD）进行了纯化和性质研究。该酶具有约80 kDa的天然分子量，而在SDS-PAGE上发现分子量为24 kDa的单体，表明它是同源四聚体。天然SOD活性染色显示一种独特的胞浆酶。在培养基中添加锰显著提高了比活力，添加铁的白色对比活力无显著影响。没有观察到生长干扰与补充培养基。体外金属去除。替代研究表明，用锰替代可以保留约85%的比活性，用铜、铁、镍或锌替代的白色并没有恢复任何显着的比活性。用原子吸收光谱仪对锰进行了鉴定，未检测到白色对应于固定其他金属元素的信号。因此，C.谷氨酸超氧化物歧化酶（MnSOD）是一种严格的（非形成型）锰超氧化物歧化酶。(c)2006年Elsevier GmbH。保留所有权利。
Superoxide dismutase (SOD) of Corynebacterium glutamicum was purified and characterized. The enzyme had a native molecular weight of about 80 kDa, whereas a monomer with molecular weight of 24 kDa was found on SDS-PAGE suggesting it to be homotetramer. The native SOD activity stained get revealed a unique cytosolic enzyme. Supplementing growth media with manganese increased the specific activity significantly, white adding iron did not result in significant difference. No growth perturbation was observed with the supplemented media.In vitro metal removal. and replacement studies revealed conservation of about 85% of the specific activity by substitution with manganese, white substitution with copper, iron, nickel or zinc did not restore any significant specific activity. Manganese was identified by atomic absorption spectrometer, white no signals corresponding to fixing other metallic elements were detected. Thus, C. glutamicum SOD could be considered a strict (non-cambiatistic) manganese superoxide dismutase (MnSOD). (c) 2006 Elsevier GmbH. AR rights reserved.