. Author manuscript; available in PMC: 2010 Jul 1.

Published in final edited form as: Chem Rev. 2009 Jul;109(7):2903–2928. doi: 10.1021/cr900021w

Table 4. TAD analogs. data from ²²⁰.

a. Uncompetitive inhibition is observed with both IMP and NAD⁺; the value of K_i with IMP as the variable substrate is shown. Note that experimental conditions were not described, so there is a concern that the the concentration of SAD was not in excess of enzyme, so that the value of K_i is an upper limit.

Compound	X	Y	hIMPDH1^a K_i μM	hIMPDH2^a K_i μM
TAD	S	N	0.7	0.43
SAD	Se	N	0.03	0.02
TFAD	S	CH	0.37	0.32
SFAD	Se	CH	0.58	1.10
FFAD	O	CH	38	56

Table 4. TAD analogs. data from 220.

Table 4. TAD analogs. data from ²²⁰.