Carboxylate group interaction diagram

Fig. 20. Schematic diagram of indirect carboxylate-zinc interactions through bridging hydroxyl groups, as observed in the (a) zinc proteases and (b) carbonic anhydrases.

Figure 6 Schematic diagram of the active site of the E. coli NADP-IDH with bound 2A,3>S-isocitrate (A) and the active site of T. thermophilus NAD-IMDH with bound 2R,3S-isopropylmalate (B). A prime indicates the residues donated from the second subunit, a, 3 refers to a- and P-carboxyl groups, respectively. The major determinants of substrate specificity are residues Seri 13 and Asnll5 in the NADP-IDH, and Glu87 and Leu90 in the NAD-IMDH, which interact with the unique y-moieties of the substrates. (Modified from Ref. 15.)...

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