caa a22 4500 475744047 CHVBK 20180406123507.0 cr unu---uuuuu 170329e20001001xx s 000 0 eng 10.1023/A:1007195130725 doi (NATIONALLICENCE)springer-10.1023/A:1007195130725 Inhibition of Octopus Glutathione Transferase by Meisenheimer Complex Analog, S-(2,4,6-trinitrophenyl) Glutathione [Elektronische Daten] [Jong-Yan Liou, Ter-Mei Huang, Gu-Gang Chang] The tight binding of Meisenheimer intermediate with octopus digestive gland glutathione transferase was analyzed with 1,3,5-trinitrobenzene, which forms a trapped Meisenheimer complex with glutathione because there is no leaving group at the ipso carbon. By steady-state enzyme kinetic analysis, an inhibition constant of 1.89 ± 0.17 μM was found for the transient formed, S-(2,4,6-trinitrophenyl) glutathione. The above inhibition constant is 407-fold smaller than the K m value for the substrate (2,4-dinitrochlorobenzene). Thus, S-(2,4,6-trinitrophenyl) glutathione is considered to be a transition-state analog. The tight binding of this inhibitor to the enzyme provides an explanation for the involvement of the biological binding effect on the rate enhancement in the glutathione transferase-catalyzed SNAr mechanism. Plenum Publishing Corporation, 2000 GST nationallicence transition-state analog nationallicence enzyme inhibition nationallicence inhibition mechanism nationallicence Meisenheimer complex nationallicence GST inhibition nationallicence Liou Jong-Yan Department of Biochemistry, National Defense Medical Center, P.O. Box 90048-501 (Neihu), 114, Taipei, Taiwan aut Huang Ter-Mei Department of Biochemistry, National Defense Medical Center, P.O. Box 90048-501 (Neihu), 114, Taipei, Taiwan aut Chang Gu-Gang Department of Biochemistry, National Defense Medical Center, P.O. Box 90048-501 (Neihu), 114, Taipei, Taiwan aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/7(2000-10-01), 615-620 0277-8033 19:7<615 2000 19 10930 https://doi.org/10.1023/A:1007195130725 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1007195130725 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Liou Jong-Yan Department of Biochemistry, National Defense Medical Center, P.O. Box 90048-501 (Neihu), 114, Taipei, Taiwan aut NATIONALLICENCE 700 1- Huang Ter-Mei Department of Biochemistry, National Defense Medical Center, P.O. Box 90048-501 (Neihu), 114, Taipei, Taiwan aut NATIONALLICENCE 700 1- Chang Gu-Gang Department of Biochemistry, National Defense Medical Center, P.O. Box 90048-501 (Neihu), 114, Taipei, Taiwan aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/7(2000-10-01), 615-620 0277-8033 19:7<615 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer