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Rossmann fold
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== Function == The function of the Rossmann fold in enzymes is to bind nucleotide cofactors. It also often contributes to substrate binding. Metabolic enzymes normally have one specific function, and in the case of [[UDP-glucose 6-dehydrogenase]], the primary function is to catalyze the two step NAD(+)-dependent oxidation of [[UDP-glucose]] into [[UDP-glucuronic acid]].<ref name="Bhattacharyya_2012">{{cite journal | vauthors = Bhattacharyya M, Upadhyay R, Vishveshwara S | title = Interaction signatures stabilizing the NAD(P)-binding Rossmann fold: a structure network approach | journal = PLOS ONE | volume = 7 | issue = 12 | pages = e51676 | year = 2012 | pmid = 23284738 | pmc = 3524241 | doi = 10.1371/journal.pone.0051676 | bibcode = 2012PLoSO...751676B | doi-access = free }}</ref> The N- and C-terminal domains of UgdG share structural features with ancient mitochondrial ribonucleases named MAR. MARs are present in lower eukaryotic microorganisms, have a Rossmannoid-fold and belong to the isochorismatase superfamily. This observation reinforces that the Rossmann structural motifs found in NAD(+)-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease.
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