High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin

High resolution crystal structures of tr

High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liganded active site

✍ Rajaram Venkatesan; Markus Alahuhta; Petri M. Pihko; Rik K. Wierenga 📂 Article 📅 2011 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 720 KB

## Abstract The key residue of the active site of triosephosphate isomerase (TIM) is the catalytic glutamate, which is proposed to be important (i) as a catalytic base, for initiating the reaction, as well as (ii) for the subsequent proton shuttling steps. The structural properties of this glutamat