Gene sequence analysis and properties of EGC, a family E (9) endoglucanase from Fibrobacter succinogenes BL2.
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.
Bera
C
C
Laboratoire de Microbiologie, INRA CR de Clermont-Ferrand-Theix, France.
Broussolle
V
V
Forano
E
E
Gaudet
G
G
D000595:Amino Acid Sequence; D000818:Animals; D002480:Cellulase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D005798:Genes, Bacterial; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology* / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D012417:Rumen / Q000382:microbiology; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013696:Temperature
D004269:DNA, Bacterial; D002480:Cellulase