Psychrophilic Enzymes: A Thermodynamic Challenge
peer reviewed Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a higher catalytic efficiency over a temperature range of roughly 0-30 degrees C and a...
Published in: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology |
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Language: | English |
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Online Access: | https://orbi.uliege.be/handle/2268/16227 https://doi.org/10.1016/S0167-4838(97)00093-9 |
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ftorbi:oai:orbi.ulg.ac.be:2268/16227 2024-04-21T07:49:30+00:00 Psychrophilic Enzymes: A Thermodynamic Challenge Gerday, Charles Aittaleb, Mohamed Arpigny, Jean Louis Baise, Etienne Chessa, Jean-Pierre Garsoux, Geneviève Petrescu, Ioan Feller, Georges 1997-10-17 https://orbi.uliege.be/handle/2268/16227 https://doi.org/10.1016/S0167-4838(97)00093-9 en eng Elsevier urn:issn:0006-3002 urn:issn:1878-2434 https://orbi.uliege.be/handle/2268/16227 info:hdl:2268/16227 doi:10.1016/S0167-4838(97)00093-9 scopus-id:2-s2.0-0030699980 info:pmid:9392521 restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess Biochimica et Biophysica Acta, 1342 (2), 119-31 (1997-10-17) 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 1997 ftorbi https://doi.org/10.1016/S0167-4838(97)00093-9 2024-03-27T14:55:01Z peer reviewed Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a higher catalytic efficiency over a temperature range of roughly 0-30 degrees C and a high thermosensitivity. The molecular characteristics of cold enzymes originating from Antarctic bacteria have been approached through protein modelling and X-ray crystallography. The deduced three-dimensional structures of cold alpha-amylase, beta-lactamase, lipase and subtilisin have been compared to their mesophilic homologs. It appears that the molecular adaptation resides in a weakening of the intramolecular interactions, and in some cases in an increase of the interaction with the solvent, leading to more flexible molecular edifices capable of performing catalysis at a lower energy cost. Article in Journal/Newspaper Antarc* Antarctic University of Liège: ORBi (Open Repository and Bibliography) Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1342 2 119 131 |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
op_collection_id |
ftorbi |
language |
English |
topic |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
spellingShingle |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire Gerday, Charles Aittaleb, Mohamed Arpigny, Jean Louis Baise, Etienne Chessa, Jean-Pierre Garsoux, Geneviève Petrescu, Ioan Feller, Georges Psychrophilic Enzymes: A Thermodynamic Challenge |
topic_facet |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a higher catalytic efficiency over a temperature range of roughly 0-30 degrees C and a high thermosensitivity. The molecular characteristics of cold enzymes originating from Antarctic bacteria have been approached through protein modelling and X-ray crystallography. The deduced three-dimensional structures of cold alpha-amylase, beta-lactamase, lipase and subtilisin have been compared to their mesophilic homologs. It appears that the molecular adaptation resides in a weakening of the intramolecular interactions, and in some cases in an increase of the interaction with the solvent, leading to more flexible molecular edifices capable of performing catalysis at a lower energy cost. |
format |
Article in Journal/Newspaper |
author |
Gerday, Charles Aittaleb, Mohamed Arpigny, Jean Louis Baise, Etienne Chessa, Jean-Pierre Garsoux, Geneviève Petrescu, Ioan Feller, Georges |
author_facet |
Gerday, Charles Aittaleb, Mohamed Arpigny, Jean Louis Baise, Etienne Chessa, Jean-Pierre Garsoux, Geneviève Petrescu, Ioan Feller, Georges |
author_sort |
Gerday, Charles |
title |
Psychrophilic Enzymes: A Thermodynamic Challenge |
title_short |
Psychrophilic Enzymes: A Thermodynamic Challenge |
title_full |
Psychrophilic Enzymes: A Thermodynamic Challenge |
title_fullStr |
Psychrophilic Enzymes: A Thermodynamic Challenge |
title_full_unstemmed |
Psychrophilic Enzymes: A Thermodynamic Challenge |
title_sort |
psychrophilic enzymes: a thermodynamic challenge |
publisher |
Elsevier |
publishDate |
1997 |
url |
https://orbi.uliege.be/handle/2268/16227 https://doi.org/10.1016/S0167-4838(97)00093-9 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biochimica et Biophysica Acta, 1342 (2), 119-31 (1997-10-17) |
op_relation |
urn:issn:0006-3002 urn:issn:1878-2434 https://orbi.uliege.be/handle/2268/16227 info:hdl:2268/16227 doi:10.1016/S0167-4838(97)00093-9 scopus-id:2-s2.0-0030699980 info:pmid:9392521 |
op_rights |
restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess |
op_doi |
https://doi.org/10.1016/S0167-4838(97)00093-9 |
container_title |
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology |
container_volume |
1342 |
container_issue |
2 |
container_start_page |
119 |
op_container_end_page |
131 |
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1796932834835824640 |