AI Article Synopsis
- The last amino acid in glucosyltransferases and galactosyltransferases shows high conservation, indicating its importance in function.
- A single amino acid change can shift the sugar donor specificity in these enzymes, demonstrating their adaptability.
- For instance, a specific mutation in ACGaT allowed it to gain new activity, while a similar change in UBGT led to decreased functionality.
Article Abstract
In comparison with the amino acid sequences of seven species of glucosyltransferases and six species of galactosyltransferases, glutamine and histidine are highly conserved as the last amino acid residue of a glycosyltransferase-specific conserved region (UDPGT) in glucosyltransferases and galactosyltransferases, respectively. Consequently, the sugar donor specificities of glycosyltransferases are successfully altered by a single amino acid point mutation. UDP-galactose:anthocyanin galactosyltransferase (ACGaT), isolated from Aralia cordata, acquired glucosyltransferase activity in addition to the inherent galactosyltransferase activity by replacing histidine with glutamine. In contrast, UDP-glucose:flavonoid glucosyltransferase (UBGT), isolated from Scutellaria baicalensis, did not acquire galactosyltransferase activity by replacing glutamine with histidine, and exhibited a remarkable decrease in glucosyltransferase activity.
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| http://dx.doi.org/10.1016/j.abb.2004.06.021 | DOI Listing |
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