Institute for the Study of Inborn Errors of Metabolism, Pontificia Universidad Javeriana, Kra 7 No. 43-82 Building 53, Room 303. Bogotá, Colombia.
Gene. 2011 Sep 15;484(1-2):26-34. doi: 10.1016/j.gene.2011.05.024. Epub 2011 Jun 12.
Fructosyltransferases (FTases) are enzymes produced by plants, fungi, and bacteria, which are responsible for the synthesis of fructooligosaccharides. In this study, we conducted a computational analysis of reported sequences for FTase from a diverse source of organisms, such as plants, fungi, and bacteria. Ninety-one proteins sequences were obtained; all belonging to the glycoside hydrolase 32 (GH32) and 68 (GH68) families. The sequences were grouped in seven clades, five for plants, one for fungi, and one for bacteria. Our findings suggest that FTases from fungi and bacteria likely evolved from dicotyledonous FTases. The analysis of catalytic domains A, D and E, which contain the amino acids involved in the catalytic binding site, allowed the identification of clade-specific conserved characteristics. The analysis of sequence motifs involved in donor/acceptor molecule affinity showed that additional sequences could be responsible for donor/acceptor molecule affinity. The correlation of this large set of FTases allowed to identify additional features that might be used for the identification and classification of new FTases, and to improve the understanding of these valuable enzymes.
果糖基转移酶（FTases）是植物、真菌和细菌产生的酶，负责合成果寡糖。在这项研究中，我们对来自不同来源的生物体（如植物、真菌和细菌）的 FTase 报告序列进行了计算分析。获得了 91 个蛋白质序列；它们均属于糖苷水解酶 32（GH32）和 68（GH68）家族。这些序列分为七个分支，五个是植物的，一个是真菌的，一个是细菌的。我们的研究结果表明，真菌和细菌的 FTase 可能是从双子叶植物的 FTase 进化而来的。对催化结构域 A、D 和 E 的分析，这些结构域包含参与催化结合位点的氨基酸，允许鉴定出具有分支特异性的保守特征。对涉及供体/受体分子亲和力的序列基序的分析表明，其他序列可能负责供体/受体分子亲和力。对这一大组 FTase 的相关性分析可以识别出可能用于鉴定和分类新的 FTase 的其他特征，并加深对这些有价值的酶的理解。
