Alteration of sugar donor specificities of plant glycosyltransferases by a single point mutation
Alteration of sugar donor specificities of plant glycosyltransferases by a single point mutation
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DOI：
10.1016/j.abb.2004.06.021
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发表时间：
2004-09-15
影响因子：
3.9
通讯作者：
Yoshikawa, T
中科院分区：
文献类型：
--
作者：
Kubo, A;Arai, Y;Yoshikawa, T
与7种葡萄糖基转移酶和6种半乳糖基转移酶的氨基酸序列相比，谷氨酰胺和组氨酸分别作为葡萄糖基转移酶和半乳糖基转移酶的糖基转移酶特异性保守区（UDPGT）的最后一个氨基酸残基高度保守。因此，糖基转移酶的糖供体特异性被单个氨基酸点突变成功地改变。UDP-半乳糖：花青素半乳糖基转移酶（ACGaT），分离自龙牙木，获得葡糖基转移酶活性，除了固有的半乳糖基转移酶活性，取代组氨酸与谷氨酰胺。与此相反，UDP-葡萄糖：类黄酮葡萄糖基转移酶（UBGT），从黄芩中分离，没有获得半乳糖基转移酶活性取代谷氨酰胺与组氨酸，并表现出显着降低葡萄糖基转移酶活性。(C)2004年爱思唯尔公司All rights reserved.
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 gal acto syltransferase 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. (C) 2004 Elsevier Inc. All rights reserved.