Linked Life Data

16413550

Source:http://linkedlifedata.com/resource/pubmed/id/16413550

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-1-31
pubmed:abstractText
Recombinant expression of the large alternansucrase (2057 amino acids) was hindered in E. coli due to poor enzyme solubility and protein degradation. The effects of deletions of the alternansucrase C-terminal CW-like and APY repeated motifs on enzyme solubility and specificity were investigated. A truncated variant deleted of the APY repeats but harboring four C-terminal CW-like repeats displayed a high specific activity and the same specificity of product synthesis as the native enzyme. It is more soluble and suffers less degradation than full length alternansucrase. Hence this truncated variant is a promising tool for the further structural and kinetic study of this interesting enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
580
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
763-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Construction of a fully active truncated alternansucrase partially deleted of its carboxy-terminal domain.
pubmed:affiliation
Ecole Supérieure de Technologie des Biomolécules de Bordeaux (ESTBB), Université Victor Segalen Bordeaux 2, 146 Rue Léo Saignat, 33076 Bordeaux Cedex, France.
pubmed:publicationType
Journal Article