Protein conformational space at the edge of allostery: turning a nonallosteric malate dehydrogenase into an “allosterized” enzyme using evolution-guided punctual mutations

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SUMMARY

    The complete process involves a set of several amino_acids, with specific roles (Burgner and Ray 1984; Clarke et_al 1986, 1988; Deng et_al 1994, 2011; McClendon et_al 2005). In struc­ tures typical of the R-active state, a mobile loop that car­ ries the substrate discriminating glutamine Q102 covers the catalytic_site, allowing its dehydration and the correct anchoring of PYR with the side chain of R171, which pro­ trudes within the catalytic_site. The authors used the recently published LDH/MalDH phylogeny (Brochier-Armanet and Madern 2021) to reveal candidate amino_acids that could be linked to . . .

     

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