来自海洋原绿球藻MIT9313的活性镍超氧化物歧化酶在体内的产生依赖于其同源肽酶。
In vivo production of active nickel superoxide dismutase from Prochlorococcus marinus MIT9313 is dependent on its cognate peptidase.
作者信息
Eitinger Thomas
机构信息
Humboldt-Universität zu Berlin, Institut für Biologie/Mikrobiologie, 10115 Berlin, Germany.
出版信息
J Bacteriol. 2004 Nov;186(22):7821-5. doi: 10.1128/JB.186.22.7821-7825.2004.
Abstract
Metal-dependent superoxide dismutases (SODs) with a specific requirement for a manganese or iron ion for catalytic activity and copper- and zinc-dependent enzymes are essential for detoxification of superoxide anion radicals. Genome sequence analyses predict the existence of a nickel-dependent enzyme (NiSOD) as the unique SOD in oxygen-evolving marine cyanobacteria. NiSOD activity was observed in Escherichia coli when sodN and sodX (encoding a putative peptidase) from Prochlorococcus marinus MIT9313 were coexpressed.
摘要
对催化活性有特定锰或铁离子需求的金属依赖性超氧化物歧化酶（SOD）以及铜锌依赖性酶对于超氧阴离子自由基的解毒至关重要。基因组序列分析预测，在进行产氧的海洋蓝细菌中存在一种镍依赖性酶（NiSOD）作为唯一的超氧化物歧化酶。当来自海洋原绿球藻MIT9313的sodN和sodX（编码一种假定的肽酶）共表达时，在大肠杆菌中观察到了NiSOD活性。
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