Dehaloperoxidase: An enzymatic Swiss army knife
Dehaloperoxidase: An enzymatic Swiss army knife
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DOI：
10.1016/j.ccr.2021.213976
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发表时间：
2021-08
影响因子：
20.6
通讯作者：
T. Malewschik;R. Ghiladi
中科院分区：
文献类型：
--
作者：
T. Malewschik;R. Ghiladi
海洋蠕虫Amphitrite ornata的血红蛋白除具有氧转运功能外，还具有多种酶活性。这种球蛋白被命名为脱卤过氧化物酶（DHP），它采用四种底物氧化机制作为对抗有毒代谢物的防御机制，包括电子（过氧化物酶和氧化酶）和O-原子（过氧合酶和加氧酶）转移。因此，DHP可以被定义为多功能催化血红蛋白。鉴于其过氧化物酶的功能已经在文献中建立，本次审查的目的是提供进一步的结构和机制的细节到其他三个活动进行DHP，特别强调其过氧合酶活性。
The hemoglobin from the marine wormAmphitrite ornatahas been found to possess multiple enzymatic activities in addition to its O2-transport function. Named dehaloperoxidase (DHP), this globin employs four mechanisms for substrate oxidation as a defense mechanism against toxic metabolites, spanning electron- (peroxidase and oxidase) and O-atom (peroxygenase and oxygenase) transfer. As such, DHP can be defined as a multifunctional catalytic hemoglobin. Given that its peroxidase function is already well established in the literature, this review aims to provide further structural and mechanistic details into the other three activities performed by DHP, with a particular emphasis on its peroxygenase activity.