Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
1997-11-6
pubmed:abstractText
The cellulosome-integrating protein CipA of Clostridium thermocellum was produced from a recombinant clone of Escherichia coli and purified by cellulose affinity and anion exchange chromatography. Two active forms of C. thermocellum endoglucanase CelD were tested for binding and hydrolytic activity on Avicel in the presence and in the absence of CipA. One was 68 kDa CelD, which contains an intact dockerin domain. The other was 65 kDa CelD, in which the dockerin domain is partially deleted. CipA promoted quantitative binding of 68 kDa CelD to Avicel and enhanced its Avicelase activity by at least ten-fold. By contrast, CipA had no effect on the activity nor on the cellulose-binding affinity of the truncated 65 kDa form. These results show that interaction between CipA and the catalytic component CelD is needed for the degradation of cellulose and confirm that the interaction is mediated by the dockerin domain of CelD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0168-1656
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-47
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Synergism between the cellulosome-integrating protein CipA and endoglucanase CelD of Clostridium thermocellum.
pubmed:affiliation
Unité de Physiologie Cellulaire, Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't