GPx7 likes to interact with the domain of PDI, and intramolecular cooperation between the two redox-active sites of PDI increases the activity of the Ero1/GPx7/PDI triplet, thereby promoting protein folding mechanisms (Wang et al., 2014) (Figure 6)
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Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis
We therefore suggest a mechanism that can be described according to the Cleland nomenclature as a combination of a random bi-uni mechanism and a ping-pong bi-bi (or uni-uni-uni-uni) mechanism in which the single product of the rate-limiting random mechanism becomes the first substrate of the ping-pong mechanism (Fig
The involvement of individual P450s in the metabolism of a given drug may be screened in vitro by means of selective functional markers, selective chemical P450 inhibitors, and P450 antibodies
