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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology: And Related Areas of Molecular Biology, Volume 76

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The existence of different conformations observed in various crystalline complexes is supported by limited proteolysis data that showed changes in loop susceptibility in solution. A study of the potential conformational alterations associated with ligand binding to the human type 2 IMPDH revealed that residues in the flap region (from residues 411 to 441) became protected from various proteases in the presence of IMP or XMP (121). NADH provided less protection and NAD did not protect at all, in accord with other binding data (16).

1 M concentration of Kþ needed for saturation the secondorder binding rate of Kþ is much faster than the binding rates for IMP or NAD at their typical $10À4 M concentrations. During steady-state turnover a significant proportion of the enzyme is in complexes with the XMP product since XMP release is partially rate limiting. This mechanism was supported by the subsequent demonstration with IMPDH from other sources that substrate inhibition by NAD is uncompetitive with respect to IMP and reflects NAD binding to EÁXMP or E-XMP* (53).

The rate of XMP release of 17 sÀ1 is eightfold greater than kcat, showing that an earlier step is rate limiting. NAD and NADH binding were also measured by changes in T. foetus IMPDH protein fluorescence (18). Interestingly the NAD binding curve was sigmoidal with a Hill coefficient of 2 suggesting cooperativity in binding. 320 V) gave similar kcat values, implying a common rate-determining step because the intrinsic rates of hydride transfer should be modulated by the magnitude of the differences in reduction potential between the substrates and products.

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