Purification, characterization and modular organization of a cellulose-binding protein, CBP105, a processive beta-1,4-endoglucanase from Cellulomonas flavigena.
A cellulose-binding protein of 105 kDa (CBP105) from Cellulomonas flavigena was purified and its gene was cloned. CBP105 is a processive endoglucanase with maximum activity on carboxymethyl cellulose (CMC) at pH 7.5 and 60 degrees C. Limited proteolysis suggested that CBP105 is composed of one catalytic domain (CD) and two carbohydrate-binding modules (CBM). The nucleotide sequence of the cbp105 gene (AY729806) indicates that CBP105 is a modular enzyme with a family 9 glycoside hydrolase CD linked to a family 3 CBM, two fibronectin III-like domains and a family 2 CBM. This structural organization may be responsible for CBP105 processive CMC degradation.
Mejia-Castillo
Teresa
T
Departamento de Biotecnología y Bioingeniería, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV-IPN), Av. IPN 2508, Col. San Pedro Zacatenco, 07360 México, DF, México.
Hidalgo-Lara
Maria Eugenia
ME
Brieba
Luis G
LG
Ortega-Lopez
Jaime
J
D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002480:Cellulase / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D040143:Cellulomonas / Q000201:enzymology* / Q000235:genetics; D002482:Cellulose / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D011485:Protein Binding
D001426:Bacterial Proteins; D002482:Cellulose; D002480:Cellulase