GENE SEQUENCE-ANALYSIS AND PROPERTIES OF EGC, A FAMILY E(9) ENDOGLUCANASE FROM FIBROBACTER-SUCCINOGENES BL2

Citation
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
Citations number
19
Categorie Soggetti
Microbiology
Journal title
ISSN journal
03781097
Volume
136
Issue
1
Year of publication
1996
Pages
79 - 84
Database
ISI
SICI code
0378-1097(1996)136:1<79:GSAPOE>2.0.ZU;2-S
Abstract
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.