来自琥珀酸丝状杆菌S85的新型E族内切葡聚糖酶EGB的基因序列及蛋白结构域分析

Gene sequence and analysis of protein domains of EGB, a novel family E endoglucanase from Fibrobacter succinogenes S85.

作者信息

Broussolle V, Forano E, Gaudet G, Ribot Y

机构信息

Laboratoire de Microbiologie, INRA CR de Clermont-Ferrand-Theix, Saint-Genès-Champanelle, France.

出版信息

FEMS Microbiol Lett. 1994 Dec 15;124(3):439-47. doi: 10.1111/j.1574-6968.1994.tb07321.x.

DOI:10.1111/j.1574-6968.1994.tb07321.x

PMID:7851752

Abstract

The endoglucanase gene (endB) of Fibrobacter succinogenes S85 encodes a protein of 555 amino acids (EGB) with a M(r) of 62,500. EGB shows homology with cellulases belonging to family E. Residues involved in the catalytic activity of CelD from Clostridium thermocellum are also found in EGB. Structure predictions suggest that EGB, like CelD, comprises a large alpha-helical catalytic domain plus a beta-strand domain of unknown function located in the N-terminal part of the protein. Construction of a phylogenetic tree of family E catalytic domains revealed that EGB is closest to a cellodextrinase from Butyrivibrio fibrisolvens.

摘要

琥珀酸纤维杆菌S85的内切葡聚糖酶基因（endB）编码一种由555个氨基酸组成的蛋白质（EGB），分子量为62,500。EGB与属于E家族的纤维素酶具有同源性。嗜热栖热菌CelD催化活性所涉及的残基在EGB中也有发现。结构预测表明，EGB与CelD一样，包含一个大的α-螺旋催化结构域以及位于蛋白质N端部分的功能未知的β-链结构域。构建E家族催化结构域的系统发育树显示，EGB与来自溶纤维丁酸弧菌的纤维二糖酶关系最为密切。