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

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Mþ activation of the Glu469Ala mutant was positively cooperative, which also suggests more than one mode of interaction. 5-fold for Vmax/Km of NAD) suggest that the cations do not directly participate in the hydride transfer step of the reaction. INOSINE 50 -MONOPHOSPHATE DEHYDROGENASE 39 However, until studies ensure that the same steps in the mechanism are rate limiting in the reactions with the various ions, the isotope effects provide limited insight into the mechanism of Mþ activation (89).

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.

8 kcal/mol (IMP bound) at 25 C] indicative of a conformational change on binding (123, 124). The authors proffered an explanation that the ligandfree enzyme exists in multiple conformational forms, which is consistent with the difficulties in crystallizing the ligand-free protein. The calorimetric results for MPA binding to the EÁIMP complex were evaluated in terms of a protein conformational distribution that persists in the binary complex. INOSINE 50 -MONOPHOSPHATE DEHYDROGENASE 33 An alignment of the B.

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