Improving the Catalytic Activity of Hyperthermophilic Pyrococcus horikoshii Prolidase for Detoxification of Organophosphorus Nerve Agents over a Broad Range of Temperatures

Figure 3

Mapping of the mutations in the monomeric structure of P. horikoshii prolidase (Ph1prol or PH0974). Mutations made in the Ph1prol are indicated by colored arrows where red indicates mutations present in Mutant no.10 (A195T/G306S-Ph1prol), orange indicates mutations in Mutant no.19 (Y301C/K342N), green indicates mutations in Mutant no.35 (E127G/E252D), and blue indicates mutations in Mutant no.72 (E36V). The domain structure of Ph1prol is presented as a ribbon drawing where the N-terminal (residues 1–120) and C-terminal (131–356) domains are labeled and are connected by a α-helical linker at residues 121–130. The putative active site pocket is located between two 3₁₀ helixes (two red helices, residues 191–195 and 281–284) (modified from [18]).