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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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Four mutations lying both near to and far from the active site were found. The authors noted that because the MPA inhibits by trapping of the E-XMP* intermediate, any mutation that decreases the accumulation of E-XMP* can result in reduced inhibition without directly modifying the MPA binding site (128). Indeed, evolution of IMPDH toward resistance to MPA may either change the MPA binding site topology or 36 MAXIM PIMKIN AND GEORGE D. MARKHAM stabilize the closed enzyme conformation which will prevent MPA binding.

Pre-steady-state studies of the NADH formation revealed that the rate of fluorescence change was smaller than that the rate of absorption increase, as seen with the T. foetus enzyme. The authors (21, 65) suggested that the fluorescence of bound NADH is quenched by stacking with the purine of XMP. Mutants of the E. coli enzyme were constructed at each of 11 evolutionarily conserved aspartate and glutamate residues before any IMPDH crystal structures were available (65). The acidic residues at the IMP and NAD binding sites were both identified.

In accord with this coupling, the wild-type enzyme-catalyzed rate of hydride transfer from 20 -deoxy-IMP decreased by >5-fold; furthermore, in the 20 -deoxy-IMP reaction both absorbance and fluorescence changes showed the same rates, suggesting that the nicotinamide and purine rings are no longer oriented to quench NADH fluorescence in the bound complex. The Asp248Ala substitution selectively impaired NAD binding, consistent with the crystallographically observed role of the corresponding residue in human IMPDH (Asp274) in binding the ribose hydroxyls of the selenazole riboside moiety in the SAD complex (31).

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