Table 1. Kinetic studies of most active compounds on thymidine phosphorylase.

Compound	Ki (μM ± SEM)a	Inhibition Type
3	176.65 ± 0.006	Uncompetitive
9	138.0 ± 0.009	Uncompetitive
14	80.5 ± 0.002	Uncompetitive
22	1.75 ± 0.009	Non-competitive
27	168.0 ± 0.003	Uncompetitive
29	159.05 ± 0.002	Uncompetitive
7-Deazaxanthine	45.66 ± 0.0009	Non-competitive