Abstract
IMP dehydrogenase (IMPDH) and GMP reductase (GMPR) have very similar structures, bind the same ligands with similar affinities and catalyze reactions involving the same covalent intermediate E-XMP*, yet with very different outcomes. Where IMPDH catalyzes the reaction of E-XMP* with water, GMPR has 蠅106 –fold selectivity for ammonia. This reaction specificity appears to derive from the dynamic motion of enzyme-bound nicotinamide cofactor.
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Schedule a callMore From: FASEB journal : official publication of the Federation of American Societies for Experimental Biology
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