Catalytic properties of the cellulose-binding endoglucanase F from Fibrobacter succinogenes S85.
The celF gene from the predominant cellulolytic ruminal bacterium Fibrobacter succinogenes encodes a 118.3-kDa cellulose-binding endoglucanase, endoglucanase F (EGF). This enzyme possesses an N-terminal cellulose-binding domain and a C-terminal catalytic domain. The purified catalytic domain displayed an activity profile typical of an endoglucanase, with high catalytic activity on carboxymethyl cellulose and barley beta-glucan. Immunoblotting of EGF and the formerly characterized endoglucanase 2 (EG2) from F. succinogenes with antibodies prepared against each of the enzymes demonstrated that EGF and EG2 contain cross-reactive epitopes. This data in conjunction with evidence that the proteins are the same size, share a 19-residue internal amino acid sequence, possess similar catalytic properties, and both bind to cellulose allows the conclusion that celF codes for EG2.
Malburg
S R
SR
Department of Microbiology, University of Guelph, Ontario, Canada.
Malburg
L M
LM
Liu
T
T
Iyo
A H
AH
Forsberg
C W
CW
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002480:Cellulase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002482:Cellulose / Q000378:metabolism; D005798:Genes, Bacterial; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D015183:Restriction Mapping; D012417:Rumen / Q000382:microbiology; D017386:Sequence Homology, Amino Acid
D002482:Cellulose; C056373:endoglucanase 2; D002480:Cellulase