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Full-Text Articles in Medicine and Health Sciences
Structural Characterization Of Cals8, A Tdp-Α-D-Glucose Dehydrogenase Involved In Calicheamicin Aminodideoxypentose Biosynthesis, Shanteri Singh, Karolina Michalska, Lance Bigelow, Michael Endres, Madan K. Kharel, Gyorgy Babnigg, Ragothaman M. Yennamalli, Craig A. Bingman, Andrzej Joachimiak, Jon S. Thorson, George N. Phillips Jr.
Structural Characterization Of Cals8, A Tdp-Α-D-Glucose Dehydrogenase Involved In Calicheamicin Aminodideoxypentose Biosynthesis, Shanteri Singh, Karolina Michalska, Lance Bigelow, Michael Endres, Madan K. Kharel, Gyorgy Babnigg, Ragothaman M. Yennamalli, Craig A. Bingman, Andrzej Joachimiak, Jon S. Thorson, George N. Phillips Jr.
Center for Pharmaceutical Research and Innovation Faculty Publications
Classical UDP-glucose 6-dehydrogenases (UGDHs; EC 1.1.1.22) catalyze the conversion of UDP-α-d-glucose (UDP-Glc) to the key metabolic precursor UDP-α-d-glucuronic acid (UDP-GlcA) and display specificity for UDP-Glc. The fundamental biochemical and structural study of the UGDH homolog CalS8 encoded by the calicheamicin biosynthetic gene is reported and represents one of the first studies of a UGDH homolog involved in secondary metabolism. The corresponding biochemical characterization of CalS8 reveals CalS8 as one of the first characterized base-permissive UGDH homologs with a >15-fold preference for TDP-Glc over UDP-Glc. The corresponding structure elucidations of apo-CalS8 and the CalS8·substrate·cofactor ternary complex (at 2.47 and 1.95 Å …