Fourquet Simon, Huang Meng-Er, D'Autreaux Benoit, Toledano Michel B
CEA, DSV, IBITECS, Laboratoire Stress Oxydants et Cancer, CEA-Saclay, Gif-sur-Yvette France.
Antioxid Redox Signal. 2008 Sep;10(9):1565-76. doi: 10.1089/ars.2008.2049.
Thiol-based peroxidases consist of the peroxiredoxins (Prx) and the related glutathione peroxidase (GPx)-like enzymes. Their catalytic function is to reduce peroxides by using the reactivity of the cysteine residue, and their presumed primary physiologic role is to protect living organisms from peroxide toxicity. However, as peroxide-metabolizing enzymes, they also regulate hydrogen peroxide (H2O2) signaling. We review here enzymatic and biochemical attributes of thiol peroxidases that specify both distinctive peroxide-scavenging functions and the property of regulating H2O2 signaling. We then discuss possible thiol peroxidase physiologic functions, based on selected observations made in microorganisms and mammals.
基于硫醇的过氧化物酶包括过氧化物还原酶(Prx)和相关的谷胱甘肽过氧化物酶(GPx)样酶。它们的催化功能是利用半胱氨酸残基的反应性来还原过氧化物,其假定的主要生理作用是保护生物体免受过氧化物毒性的影响。然而,作为过氧化物代谢酶,它们也调节过氧化氢(H2O2)信号传导。我们在此综述硫醇过氧化物酶的酶学和生化特性,这些特性既明确了独特的过氧化物清除功能,又明确了调节H2O2信号传导的特性。然后,我们根据在微生物和哺乳动物中进行的选定观察结果,讨论硫醇过氧化物酶可能的生理功能。