- Encompasses the newest advances within the box.
- New sequence editor, Daniel Purich, is a well known biochemist and enzymologist.
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology: And Related Areas of Molecular Biology, Volume 76
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.
Gan et al. proposed that the movement of the flap in and out of the NAD site is the necessary conformational change converting the enzyme from a dehydrogenase to a hydrolase. A remarkable but unexplained phenomenon is the paucity of tryptophan in IMPDH proteins from archaea, bacteria, and eucarya—most available IMPDH sequences have no tryptophan or a single tryptophan residue. It would seem unlikely that this deficit would be coincidental across evolution, but no rationale is obvious. The fluorescence from the multiple tryptophans naturally present in the T.
The variation in affinity of MMP for different IMPDH illustrates the potential for development of species-selective inhibitors (Table 1). A purine ring expanded (“fat base”) nucleoside imidazo[4, 5-e]diazapine, in which an additional methylene group creates a seven-member ring in place of the six-member system of XMP, is a potent slow-binding inhibitor of the E. coli and human enzymes; the kinetics may reflect formation of a covalent adduct which is labile upon protein denaturation (66). B. NAD ANALOGS The efforts to develop clinically useful NAD analogs with selectivity for IMPDH have been extensively reported (4, 67).