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Figure 7
Proposal for the mechanism of D-T6P inhibition in TalBF178Y. Proton abstraction from the iminium ion yields the α-hydroxyenamine. This step is proposed to be catalysed by the side chain of Tyr178. The α-hydroxyenamine undergoes a rearrangement to a stable α-ketoamine. The furanose ring is closed via hemiacetal formation and remains bound covalently via the C2 atom to the active-site residue Lys132.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 72| Part 4| April 2016| Pages 467-476
doi:10.1107/S2059798316001170
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