Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Joucla G,Pizzut S,Monsan P,Remaud-Simeon Mdoi
10.1016/j.febslet.2006.01.001keywords:
subject
Has Abstractpub_date
2006-02-06 00:00:00pages
763-8issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(06)00005-6journal_volume
580pub_type
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