Reference : Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/16023
Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase
English
D'Amico, Salvino [Université de Liège - ULg > > GIGA-Research >]
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 >]
2002
Biologia
Slovak Academic Press Ltd
57
Suppl. 11
213-219
Yes (verified by ORBi)
International
0006-3088
Bratislava
[en] extremophiles ; protein engineering ; microcalorimetry
[en] The heat-labile alpha-amylase from an Antarctic bacterium is the largest known protein that unfolds reversibly according to a two-state transition, as shown by differential scanning calorimetry. Mutants of this enzyme were produced, carrying intended additional weak interactions of a type found in thermostable alpha-amylases. It is shown that single amino acid side chain substitutions can significantly modify the melting point T-m, the calorimetric enthalpy DeltaH(cal), the cooperativity and reversibility of unfolding, the thermal inactivation rate constant, and the kinetic parameters k(cat) and K-m. Although all mutations were located far from the active site, their overall trend is to decrease both k(cat) and K-m, probably by making the molecule more rigid, but this protects mutants against thermal inactivation.
http://hdl.handle.net/2268/16023

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
Biologia_2002.pdfPublisher postprint162.09 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.