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  • Title: Single amino acid mutations of Medicago glycosyltransferase UGT85H2 enhance activity and impart reversibility.
    Author: Modolo LV, Escamilla-Treviño LL, Dixon RA, Wang X.
    Journal: FEBS Lett; 2009 Jun 18; 583(12):2131-5. PubMed ID: 19500551.
    Abstract:
    The glycosyltransferase UGT85H2 from Medicago truncatula catalyzes glucosylation of the (iso)flavonoids kaempferol and biochanin A. Structure-based mutagenesis of UGT85H2 was carried out to explore the roles of amino acids involved in substrate binding. Substitution of Ile305 by threonine increased catalytic efficiency 37- or 19-fold with kaempferol or biochanin A as acceptor, respectively. A point mutation V200E also dramatically improved the turnover rate and catalytic efficiency by 15-fold for kaempferol and 54-fold for biochanin A. More interestingly, this single mutation (V200E) conferred reversibility in the glycosyltransfer reaction, indicating that Glu200 is a key determinant for the deglycosylation function.
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