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We determined the crystal structure of EcL-DER to elucidate protein function and substrate specificity. Unlike other asp/glu racemases, EcL-DER has an unbalanced pair of catalytic residues, Thr83/Cys197, at the active site that is crucial for l- to d-unidirectional racemase activity. EcL-DER exhibited racemase activity for both l-glutamate and l-aspartate, but had threefold higher activity for l-glutamate...
We determined the crystal structure of EcL‐DER to elucidate protein function and substrate specificity. Unlike other asp/glu racemases, EcL‐DER has an unbalanced pair of catalytic residues, Thr83/Cys197, at the active site that is crucial for l‐ to d‐unidirectional racemase activity. EcL‐DER exhibited racemase activity for both l‐glutamate and l‐aspartate, but had threefold higher activity for l‐glutamate...
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