Linked Life Data

11311718

Source:http://linkedlifedata.com/resource/pubmed/id/11311718

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-4-20
pubmed:databankReference
pubmed:abstractText
Molecular cloning and cDNA sequencing analysis were used to elucidate the primary structure of a cellulase-like structure from the white-rot fungus Coriolus versicolor. The cDNA of interest was isolated from a cDNA library obtained from C. versicolor mycelia grown on cellulase inducer medium. A pattern search showed that this cellulase belongs to the glycosyl hydrolases family 6. From the deduced amino acid sequence, models of the binding and catalytic domains were built by homology modelling. The constructed models present a typical cellulose-binding domain at the N-terminal region, a rich Pro, Ser, Thr linker peptide, and a catalytic domain at the C-terminus region.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0141-8130
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
285-92
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Primary structure deduction and molecular modelling from a cDNA of a cellobiohydrolase-like protein from the white-rot fungus Coriolus versicolor.
pubmed:affiliation
INETI/DB/UTPAM, Edifício F, Estrada do Paço do Lumiar 1649-038, Lisbon, Portugal. carlos.novo@mail.ineti.pt
pubmed:publicationType
Journal Article