Xian M, Wang K, Chen X, Hou Y, McGill A, Zhou B, Zhang Z Y, Cheng J P, Wang P G
Department of Chemistry, Wayne State University, Detroit, Michigan, 48202, USA.
Biochem Biophys Res Commun. 2000 Feb 16;268(2):310-4. doi: 10.1006/bbrc.2000.2117.
The homogeneous recombinant mammalian protein tyrosine phosphatase 1B (PTP1B) and Yersinia protein tyrosine phosphatase (PTPase) are inactivated by a series of low-molecular-weight S-nitrosothiols. These compounds exhibited different inhibitory activities in a time- and concentration-dependent manner with second-order rate constants (k(inact)/K(I)) ranging from 37 to 113 M(-1) min(-1) against mammalian PTP1B and from 66 to 613 M(-1) min(-1) against Yersinia PTPase. Furthermore, the inactivation of Yersinia PTPase by S-nitrosylated protein:S-nitroso human serum albumin was investigated. Both single-S-nitrosylated and poly-S-nitrosylated human serum albumin show good inhibitory ability to Yersinia PTPase. The second-order rate constants are 472 and 1188 M(-1) min(-1), respectively. This result indicates a possibility that S-nitrosylated albumin in vivo may function as an inhibitor for a variety of cysteine-dependent enzymes.
均一的重组哺乳动物蛋白酪氨酸磷酸酶1B（PTP1B）和耶尔森氏菌蛋白酪氨酸磷酸酶（PTPase）可被一系列低分子量的S-亚硝基硫醇灭活。这些化合物以时间和浓度依赖性方式表现出不同的抑制活性，对哺乳动物PTP1B的二级速率常数（k（inact）/K（I））范围为37至113 M⁻¹ min⁻¹，对耶尔森氏菌PTPase的二级速率常数范围为66至613 M⁻¹ min⁻¹。此外，还研究了S-亚硝基化蛋白：S-亚硝基人血清白蛋白对耶尔森氏菌PTPase的灭活作用。单S-亚硝基化和多S-亚硝基化的人血清白蛋白对耶尔森氏菌PTPase均显示出良好的抑制能力。二级速率常数分别为472和1188 M⁻¹ min⁻¹。该结果表明体内S-亚硝基化白蛋白可能作为多种半胱氨酸依赖性酶的抑制剂发挥作用。
