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Arch Biochem Biophys. 2004 Sep 15;429(2):198-203.

Alteration of sugar donor specificities of plant glycosyltransferases by a single point mutation.

Author information

1
School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo, 108-8641, Japan.

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.

PMID:
15313223
DOI:
10.1016/j.abb.2004.06.021
[Indexed for MEDLINE]

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