Reference : The precursor of a psychrophilic alpha-amylase: structural characterization and insights...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/15769
The precursor of a psychrophilic alpha-amylase: structural characterization and insights into cold adaptation
English
Claverie, P. [> > > >]
Vigano, C. [> > > >]
Ruysschaert, J. M. [> > > >]
Gerday, Charles mailto [Université de Liège - ULg > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences) >]
Feller, Georges mailto [Université de Liège - ULg > Département des sciences de la vie > Labo de biochimie >]
30-Jul-2003
Biochimica et Biophysica Acta-Proteins and Proteomics
Elsevier Science Bv
1649
2
119-122
Yes (verified by ORBi)
International
1570-9639
Amsterdam
[en] alpha-amylase ; psychrophile ; autotransporter ; microcalorimetry ; infrared spectroscopy
[en] The alpha-amylase precursor from the bacterium Pseudoalteromonas haloplanktis possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation. Unlike the predicted beta-barrel of autotransporters, this C-terminal propeptide displays a noticeable alpha-helix content. It is connected to the enzyme by a disordered linker and has no significant interaction with the catalytic domain. The microcalorimetric pattern of the precursor also demonstrates that the stability of protein domains may evolve differently. (C) 2003 Elsevier B.V. All rights reserved.
http://hdl.handle.net/2268/15769

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
BBA_2003_Ct.pdfPublisher postprint152.19 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.