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Modification of halogen specificity of a vanadium-dependent bromoperoxidase

机译:钒依赖性溴过氧化物酶的卤素特异性的修饰

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摘要

The halide specificity of vanadium-dependent bromoperoxidase (BPO) from the marine algae, Corallina pilulifera, has been changed by a single amino acid substitution. The residue R397 has been substituted by the other 19 amino acids. The mutant enzymes R397W and R397F showed significant chloroperoxidase (CPO) activity as well as BPO activity. These mutant enzymes were purified and their properties were investigated. The maximal velocities of CPO activities of the R397W and R397F enzymes were 31.2 and 39.2 units/mg, and the Km values for Cl− were 780 mM and 670 mM, respectively. Unlike the native enzyme, both mutant enzymes were inhibited by NaN3. In the case of the R397W enzyme, the incorporation rate of vanadate into the active site was low, compared with the R397F and the wild-type enzyme. These results supported the existence of a specific halogen binding site within the catalytic cleft of vanadium haloperoxidases.
机译:来自海藻Corallina pilulifera的钒依赖性溴过氧化物酶(BPO)的卤化物特异性已通过单个氨基酸取代而改变。残基R397已被其他19个氨基酸取代。突变酶R397W和R397F表现出显着的氯过氧化物酶(CPO)活性以及BPO活性。纯化这些突变酶并研究其性质。 R397W和R397F酶的CPO活性最高速度分别为31.2和39.2单位/ mg,Cl-的Km值分别为780 mM和670 mM。与天然酶不同,两种突变酶均被NaN3抑制。在R397W酶的情况下,与R397F和野生型酶相比,钒酸盐进入活性位点的比率低。这些结果支持在钒卤代过氧化物酶的催化裂隙内存在特定的卤素结合位点。

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