Lankin V Z, Shumaev K B, Tikhaze A K, Kurganov B I
Russian Cardiology Research and Production Center, Ministry of Healthcare of the Russian Federation, Moscow, 121552, Russia.
Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology", Russian Academy of Sciences, Moscow, 119071, Russia.
Dokl Biochem Biophys. 2017 Jul;475(1):287-290. doi: 10.1134/S1607672917040123. Epub 2017 Sep 2.
Se-containing glutathione peroxidase (GSH-Px) is one of the key enzymes of the body's antioxidant system. The kinetic characteristics of GSH-Px (substrate is tert-butyl hydroperoxide) after modification of the enzyme by various concentrations of natural dicarbonyls (glyoxal, methylglyoxal, malonic dialdehyde) were studied. It was shown that dicarbonyls affected both K and V for GSH-Px. It is suggested that the effect of various dicarbonyls on GSH-Px depends on the molecular mechanisms of their interaction with the amino acid residues of the enzyme.
含硒谷胱甘肽过氧化物酶（GSH-Px）是人体抗氧化系统的关键酶之一。研究了不同浓度的天然二羰基化合物（乙二醛、甲基乙二醛、丙二醛）对GSH-Px（底物为叔丁基过氧化氢）进行修饰后该酶的动力学特性。结果表明，二羰基化合物对GSH-Px的Km和Vmax均有影响。推测不同二羰基化合物对GSH-Px的影响取决于它们与酶氨基酸残基相互作用的分子机制。
