May 4, 2018Volume 8, Issue 5Pages 3733-4734
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The C-terminal tail of 2-deoxyribose-5-phosphate aldolase (DERA), a triosephosphate isomerase (TIM) barrel-fold enzyme catalyzing C­–C bond formation, samples various conformations in solution. Using NMR and molecular dynamics, we show that the catalytically important C-terminal tyrosine (Y259) enters the active site transiently. The Y259 sidechain hydroxyl group is a crucial part of the active-site, enabling fast reversible aldol-condensation of acetaldehyde and glyceraldehyde-3-phosphate, generating deoxyribose-5-phosphate.

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