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a worth is a little bit larger for Cd-NagA than for Zn-NagA, as expected with the tendency of zinc to lower the p

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enzyme) in the adjacent subunit ion-pairs Together with the phosphate moiety of your substrate (10). It's unlikely this arginine residue could lead on the diminution in k

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The specific role on the steel cofactor is of distinct fascination for NagA because the two crystal structures readily available for the enzyme from E. coli

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cat vs. pH-profile revealed in Determine 2A for Zn-NagA was fit to equation 3 and these final results point out which the deprotonation of one acid using a kinetic p

Mutation of the residue to either glutamine or alanine ends in mutant enzymes which have missing an important quantity of catalytic activity. The value of k

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