Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.

38 Thus, the mechanistic differences between the uncatalyzed hydrolyses of phosphate mono-, di-, and triesters can be quite significant in terms of the nature of the transition states involved.

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A large binding site can potentially allow for other types of interactions, such as hydrophobic or hydrogen bonding contacts, that might be significant for substrate recognition.

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