Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2048603 | FEBS Letters | 2009 | 5 Pages |
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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Authors
Luzia V. Modolo, Luis L. Escamilla-TreviƱo, Richard A. Dixon, Xiaoqiang Wang,