Tremblay H, Blanchard J, Brzezinski R
Département de biologie, Faculté des sciences, Université de Sherbrooke, Canada.
Can J Microbiol. 2000 Oct;46(10):952-5.
The 3D structure-oriented alignment of the primary sequences of fourteen chitosanases, mainly of bacterial origin and belonging to families 46 and 80 of glycoside hydrolases, resulted in the identification of the following pattern common to all these enzymes: E-[DNQ]-x(8,17)-Y-x(7)-D-x-[RD]-[GP]-x-[TS]-x(3)-[AIVFLY]-G- x(5,11)-D. This pattern is proposed as the molecular signature of the chitosanases from families 46 and 80. It includes several amino acids essential for enzyme activity and (or) stability as shown by site-directed mutagenesis studies on the chitosanase from Streptomyces sp. N174. In particular, it includes two carboxylic residues directly involved in catalysis. We suggest that there is a continuum of sequence similarity between all the analyzed chitosanases, and that all these enzymes should probably be classified in one family.
对主要来源于细菌且属于糖苷水解酶家族46和80的14种壳聚糖酶的一级序列进行基于三维结构的比对,结果鉴定出所有这些酶共有的以下模式:E-[DNQ]-x(8,17)-Y-x(7)-D-x-[RD]-[GP]-x-[TS]-x(3)-[AIVFLY]-G-x(5,11)-D。该模式被提议作为家族46和80中壳聚糖酶的分子特征。如对链霉菌属N174壳聚糖酶进行的定点诱变研究所表明的,它包括几个对酶活性和(或)稳定性至关重要的氨基酸。特别是,它包括两个直接参与催化的羧基残基。我们认为,所有分析的壳聚糖酶之间存在序列相似性的连续性,并且所有这些酶可能都应归为一个家族。