Studies on the possible mechanism of inactivation of phenylalanine hydroxylase by destructive oxygen species.

R M Fink, E F Elstner
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引用次数: 5

Abstract

The enzymic hydroxylation of phenylalanine by phenylalanine hydroxylase (E.C. 1.14.16.1.) in vitro is dependent on the presence of hydrogen peroxide removing processes. The loss of phenylalanine hydroxylase activity can be prevented to the same extent by catalase as well as the presence of optimized amounts of both peroxidase and superoxide dismutase. Peroxidase alone exhibited only two third of the maximal protective effect of catalase whereas superoxide dismutase alone was not able to exert any protective influence on phenylalanine hydroxylase. These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.

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破坏性氧对苯丙氨酸羟化酶失活可能机制的研究。
在体外,苯丙氨酸羟化酶(E.C. 1.14.16.1.)对苯丙氨酸的酶羟基化作用依赖于过氧化氢去除过程的存在。苯丙氨酸羟化酶活性的丧失可以通过过氧化氢酶以及优化量的过氧化物酶和超氧化物歧化酶的存在来防止。单独的过氧化物酶仅表现出过氧化氢酶最大保护作用的三分之二,而单独的超氧化物歧化酶不能对苯丙氨酸羟化酶产生任何保护作用。这些发现表明,在没有过氧化氢去除反应的情况下,苯丙氨酸羟化的终止可能是由于在H2O2和四氢蝶呤辅助因子存在下,苯丙氨酸羟化酶的活性位点铁产生了破坏性的氧。
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