Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase
peer reviewed 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 t...
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2002
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ftorbi:oai:orbi.ulg.ac.be:2268/16023 2024-10-20T14:04:18+00:00 Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase D'Amico, Salvino Gerday, Charles Feller, Georges 2002 https://orbi.uliege.be/handle/2268/16023 en eng Slovak Academic Press Ltd urn:issn:0006-3088 urn:issn:1336-9563 https://orbi.uliege.be/handle/2268/16023 info:hdl:2268/16023 restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess Biologia, 57 (Suppl. 11), 213-219 (2002) extremophiles protein engineering microcalorimetry Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire journal article http://purl.org/coar/resource_type/c_6501 info:eu-repo/semantics/article peer reviewed 2002 ftorbi 2024-09-27T07:01:35Z peer reviewed 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. Article in Journal/Newspaper Antarc* Antarctic University of Liège: ORBi (Open Repository and Bibliography) Antarctic |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
op_collection_id |
ftorbi |
language |
English |
topic |
extremophiles protein engineering microcalorimetry Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
spellingShingle |
extremophiles protein engineering microcalorimetry Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire D'Amico, Salvino Gerday, Charles Feller, Georges Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase |
topic_facet |
extremophiles protein engineering microcalorimetry Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed 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. |
format |
Article in Journal/Newspaper |
author |
D'Amico, Salvino Gerday, Charles Feller, Georges |
author_facet |
D'Amico, Salvino Gerday, Charles Feller, Georges |
author_sort |
D'Amico, Salvino |
title |
Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase |
title_short |
Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase |
title_full |
Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase |
title_fullStr |
Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase |
title_full_unstemmed |
Structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase |
title_sort |
structural determinants of cold adaptation and stability in a psychrophilic alpha-amylase |
publisher |
Slovak Academic Press Ltd |
publishDate |
2002 |
url |
https://orbi.uliege.be/handle/2268/16023 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biologia, 57 (Suppl. 11), 213-219 (2002) |
op_relation |
urn:issn:0006-3088 urn:issn:1336-9563 https://orbi.uliege.be/handle/2268/16023 info:hdl:2268/16023 |
op_rights |
restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess |
_version_ |
1813453171820855296 |