An Unusual Dehalogenating Peroxidase from the Marine Terebellid Polychaete Amphitrite ornata(*)
An Unusual Dehalogenating Peroxidase from the Marine Terebellid Polychaete Amphitrite ornata(*)
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来自海洋Terebellid Polychaete Amphitrite ornata 的一种不寻常的脱卤过氧化物酶(*)
DOI：
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发表时间：
1996
影响因子：
4.8
通讯作者：
C. R. Lovell
中科院分区：
文献类型：
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作者：
Y. Chen;S. Woodin;D. Lincoln;C. R. Lovell
terebellid polychae Amphitrite ornata不产生可检测到的挥发性卤代次生代谢物，但经常栖息在被人为或生物卤代芳香族化合物严重污染的沿海海洋沉积物中。这种动物含有高水平的两种非常罕见的酶，脱卤过氧化物酶。我们纯化并部分表征了其中的一种去卤素过氧化物酶DHP I。DHP I是一种血红素酶（M = 30,790），由两个相同的亚基（M = 15,529）组成，富含天冬氨酸（+天冬酰胺）和谷氨酸（+谷氨酰胺）。这种酶能将三卤代苯酚，如2,4,6-三溴苯酚，转化为二卤代醌。该反应的最佳pH为5.0。DHP I对二卤代和单卤代酚也有活性，并能氧化溴、氯和氟酚。我们已经在其他动物多毛动物中发现了类似的去盐过氧化物酶活性，包括产生盐代谢物的物种。
The terebellid polychaete Amphitrite ornata produces no detectable volatile halogenated secondary metabolites, but frequently inhabits coastal marine sediments heavily contaminated with anthropogenic or biogenic haloaromatic compounds. This animal contains high levels of two very unusual enzymes, dehalogenating peroxidases. We have purified and partially characterized one of these dehaloperoxidases, DHP I. DHP I is a heme enzyme (M = 30,790) composed of two identical subunits (M = 15,529) and is very rich in the amino acids aspartic acid (+ asparagine) and glutamic acid (+ glutamine). The enzyme converts trihalogenated phenols, such as 2,4,6-tribromophenol, into dihalogenated quinones. The optimum pH for this reaction is 5.0. DHP I is also active against di- and monohalogenated phenols and will oxidize bromo-, chloro-, and fluorophenols. We have identified similar dehaloperoxidase activities in other infaunal polychaetes, including halometabolite-producing species.