CHARACTERIZATION OF A MANGANESE-CONTAINING CATALASE FROM THE OBLIGATE THERMOPHILE THERMOLEOPHILUM-ALBUM
CHARACTERIZATION OF A MANGANESE-CONTAINING CATALASE FROM THE OBLIGATE THERMOPHILE THERMOLEOPHILUM-ALBUM
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DOI：
10.1128/jb.168.2.563-567.1986
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发表时间：
1986-11-01
影响因子：
3.2
通讯作者：
PERRY, JJ
中科院分区：
文献类型：
--
作者：
ALLGOOD, GS;PERRY, JJ
一种含锰的过氧化氢酶已被表征为来自嗜热菌（Thermoleophilum album NM），嗜热菌（Thermoleophilum album NM）是一种革兰氏阴性好氧细菌，专性用于嗜热性和正烷烃底物。在百草枯（2.5 μ M）（一种产生超氧化物的毒物）存在下生长，细胞中过氧化氢酶的水平增加了约9倍。超氧化物歧化酶水平不受该化合物的影响。该酶是从百草枯存在下生长的培养物中纯化的，纯度大于95%，Mr为141，000。该酶由四个亚基组成，每个亚基的Mr为34，000。每个亚基存在1.4 +/-0.4个锰原子。过氧化氢酶对过氧化氢的Km为15 mM，Vmax为11 mM/mg。过氧化物酶活性，如用对苯二胺测量的，与过氧化氢酶共纯化。血红素过氧化氢酶抑制剂对T.蛋白酶过氧化氢酶的最适pH为8 ~ 9。该酶在pH 6.5至11范围内稳定，在25至80 ℃的测定温度下保持活性。过氧化氢酶在60 ℃下孵育24小时是稳定的。
A manganese-containing catalase has been characterized from Thermoleophilum album NM, a gram-negative aerobic bacterium obligate for thermophily and n-alkane substrates. The level of catalase in cells was increased about ninefold by growth in the presence of paraquat (2.5 microM), a superoxide-generating toxicant. Superoxide dismutase levels were unaffected by this compound. The enzyme was purified from cultures grown in the presence of paraquat to greater than 95% homogeneity and had an Mr of 141,000. The enzyme was composed of four subunits, and each had an Mr of 34,000. There were 1.4 +/- 0.4 atoms of manganese present per subunit. The catalase had a Km for hydrogen peroxide of 15 mM and a Vmax of 11 mM/mg. Peroxidase activity, as measured with p-phenylenediamine, copurified with the catalase. Inhibitors of heme-catalase were weak inhibitors of the T. album enzyme. The optimum pH for catalase activity was 8 to 9. The enzyme was stable from pH 6.5 to 11 and retained activity at assay temperatures from 25 to 80 degrees C. The catalase was stable for 24 h of incubation at 60 degrees C.