Structural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH)

@inproceedings{Unterlass2017StructuralII,
  title={Structural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH)},
  author={Judith E Unterlass and Robert J. Wood and Arnaud Basl{\'e} and Julie A. Tucker and C{\'e}line Cano and Martin M.E. Noble and Nicola J Curtin},
  booktitle={Oncotarget},
  year={2017}
}
Cancer cells reprogram their metabolism and energy production to sustain increased growth, enable metastasis and overcome resistance to cancer treatments. Although primary roles for many metabolic proteins have been identified, some are promiscuous in regards to the reaction they catalyze. To efficiently target these enzymes, a good understanding of their enzymatic function and structure, as well as knowledge regarding any substrate or catalytic promiscuity is required. Here we focus on the… CONTINUE READING
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