Bera C, Broussolle V, Forano E, Gaudet G
Laboratoire de Microbiologie, INRA CR de Clermont-Ferrand-Theix, France.
FEMS Microbiol Lett. 1996 Feb 1;136(1):79-84. doi: 10.1016/0378-1097(95)00496-3.
The endoglucanase gene (endC) of Fibrobacter succinogenes BL2 encodes a protein of 620 amino acids (EGC) that shows similarity with family E1 cellulases, and particularly with EGB from F. succinogenes S85. Alignment of the amino acid sequence of family E1 cellulases revealed that EGC is composed of a N-terminal domain and a large catalytic domain of 453 residues containing an extension of 60 residues at its C-terminal part which is not present in other family E1 enzymes. EGC shows the same substrate specificity as EGB, and is also inhibited by EDTA. However, its optimal pH (7.0) and temperature (37 degrees C) for activity are different.
琥珀酸丝状杆菌BL2的内切葡聚糖酶基因（endC）编码一种由620个氨基酸组成的蛋白质（EGC），该蛋白质与E1家族纤维素酶相似，尤其与琥珀酸丝状杆菌S85的EGB相似。E1家族纤维素酶氨基酸序列比对显示，EGC由一个N端结构域和一个由453个残基组成的大催化结构域组成，其C端部分有60个残基的延伸，这在其他E1家族酶中不存在。EGC与EGB具有相同的底物特异性，并且也受EDTA抑制。然而，其活性的最适pH（7.0）和温度（37摄氏度）不同。
