C. Bera et al., GENE SEQUENCE-ANALYSIS AND PROPERTIES OF EGC, A FAMILY E(9) ENDOGLUCANASE FROM FIBROBACTER-SUCCINOGENES BL2, FEMS microbiology letters, 136(1), 1996, pp. 79-84
The endoglucanase gene (endC) of Fibrobacter succinogenes BL2 encodes
a protein of 620 amino acids (EGC) that shows similarity with family E
1 cellulases, and particularly with EGB from F. succinogenes S85. Alig
nment of the amino acid sequence of family E1 cellulases revealed that
EGC is composed of a N-terminal domain and a large catalytic domain o
f 453 residues containing an extension of 60 residues at its C-termina
l part which is not present in other family E1 enzymes. EGC shows the
same substrate specificity as EGB, and is also inhibited by EDTA. Howe
ver, its optimal pH (7.0) and temperature (37 degrees C) for activity
are different.