- Encompasses the most recent advances within the box.
- New sequence editor, Daniel Purich, is a well known biochemist and enzymologist.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology: And Related Areas of Molecular Biology, Volume 76
Mutations of other residues that partake in binding IMP (Met70Ala, Tyr111Ala, and Lys409Ala) yielded low-activity proteins with increased Km values. A Ser329Ala mutation increased the Km for both IMP and NAD without altering kcat. Mutations of residues near the purine in E-XMP* (Thr333 whose side chain OH is hydrogen bonded to the side chain of Gln441) yielded 56 to 200-fold decreases in kcat with a selective increase in the Km of NAD. Thr333 and Gln441 were proposed to catalyze the hydrolysis of E-XMP* (101), although based on typical pKa values no chemical mechanism is obvious.
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).
However, equilibrium studies with the A. aerogenes IMPDH showed that IMP binding was not altered by Kþ. Equilibrium binding studies with the human type 2 protein showed that IMP bound at a stoichiometry of four sites per tetramer and the affinity was INOSINE 50 -MONOPHOSPHATE DEHYDROGENASE 19 only enhanced two-fold by Kþ (16). Significant NAD binding was not detected for either the A. aerogenes or human type 2 protein, but NADH was found to bind to the latter protein, and all substrates/products bind individually to the T.