Figure 10 | Scientific Reports

Figure 10

From: Implications of differential peroxyl radical-induced inactivation of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase for the pentose phosphate pathway

Figure 10

In silico analysis of the 3-D structure of G6PDH (built as described in Materials and methods section) and the crystal structure of 6PGDH (PDBid: 2ZYD). The proteins are presented as dimers, with the surface of catalytic, substrate and NADP+ binding sites per monomers colored based on the electrostatic potential, with a gradient from -5 kT/e (red) to 5 kT/e (blue). Amino acids involved in the catalytic mechanisms are presented; His239 for G6PDH (panel A, left) and Lys183 for 6PGDH (panel B, left). For both enzymes, residues detected as oxidized species with a modification level > 10% are presented (panels A and B, at right). Panel (C) shows the crystal structure of 6PGDH highlighting Tyr447, Tyr453, and Trp466, which are located at the carboxyl terminus of each monomer, which is shared with the other monomer. The table presented in panel (C) shows the amino acids included in this region, between Asn439 and Asp468.

Back to article page