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Understanding the contribution of synonymous mutations to human disease

They suggested that in BlGGT, Thr399 is activated by the OG atom of another Thr417 in lieu of a water molecule as is the case of EcGGT (Figure 3)

Some of the structural characteristics of GSTs are also observed in other GSH-dependent proteins, such as glutaredoxin, suggesting a strong evolutionary pressure to retain structural motifs involved in binding GSH at the active site [3,5,17]