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. Author manuscript; available in PMC: 2009 Aug 20.
Published in final edited form as: Chem Rev. 2006 Aug;106(8):3443–3467. doi: 10.1021/cr050317n

Figure 22.

Figure 22

Methylphosphonate substitution studies on UDG catalysis and transition state inhibitor binding. (A) The relative kcat values for the fast (f) and slow (s) migrating methylphosphonate stereoisomers are indicated. (B) 1-Azadeoxyribose oxacarbenium ion mimics. Each phosphodiester linkage was substituted with a methylphosphonate group to remove the charge, and the relative KD values compared to the all phosphodiester analogue were measured.