Janecek S, Svensson B, Russell R R
Institute of Microbiology, Slovak Academy of Sciences, Bratislava, Slovak Republic.
FEMS Microbiol Lett. 2000 Nov 1;192(1):53-7. doi: 10.1111/j.1574-6968.2000.tb09358.x.
Glucosyltransferases of oral streptococci, dextransucrases and alternansucrase of Leuconostoc mesenteroides, collectively referred to as glucansucrases, are large extracellular enzymes that synthesise glucans with a variety of structures and properties. A characteristic of all these glucansucrases is the possession of a C-terminal domain consisting of a series of tandem amino acid repeats. These repeat units are thought to interact with glucan but closely resemble the cell wall binding domain motif found in choline binding proteins in Streptococcus pneumoniae and surface-located proteins in a range of other bacteria. Analysis of dextransucrase and alternansucrase sequences has now shown that they also contain these repeat motifs in the N-terminal region, raising questions about their evolutionary origin and functional importance.
口腔链球菌的葡糖基转移酶、肠系膜明串珠菌的葡聚糖蔗糖酶和交替蔗糖酶,统称为葡聚糖蔗糖酶,是大型细胞外酶,可合成具有多种结构和特性的葡聚糖。所有这些葡聚糖蔗糖酶的一个特点是拥有一个由一系列串联氨基酸重复序列组成的C端结构域。这些重复单元被认为与葡聚糖相互作用,但与肺炎链球菌中胆碱结合蛋白和一系列其他细菌中位于表面的蛋白所发现的细胞壁结合结构域基序非常相似。对葡聚糖蔗糖酶和交替蔗糖酶序列的分析现已表明,它们在N端区域也含有这些重复基序,这引发了关于它们进化起源和功能重要性的问题。