Stepwise Adaptations to Low Temperature as Revealed by Multiple Mutants of Psychrophilic α-Amylase from Antarctic Bacterium*

Background: Cold-adapted enzymes remain catalytically active at low temperatures.

Bibliographic Details
Published in:Journal of Biological Chemistry
Main Authors: Cipolla, Alexandre, D'Amico, Salvino, Barumandzadeh, Roya, Matagne, André, Feller, Georges
Format: Text
Language:English
Published: American Society for Biochemistry and Molecular Biology 2011
Subjects:
Protein Structure and Folding
Antarctic
Antarc*
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3207396
http://www.ncbi.nlm.nih.gov/pubmed/21900238
https://doi.org/10.1074/jbc.M111.274423
id ftpubmed:oai:pubmedcentral.nih.gov:3207396
record_format openpolar
spelling ftpubmed:oai:pubmedcentral.nih.gov:3207396 2023-05-15T13:48:01+02:00 Stepwise Adaptations to Low Temperature as Revealed by Multiple Mutants of Psychrophilic α-Amylase from Antarctic Bacterium* Cipolla, Alexandre D'Amico, Salvino Barumandzadeh, Roya Matagne, André Feller, Georges 2011-11-04 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3207396 http://www.ncbi.nlm.nih.gov/pubmed/21900238 https://doi.org/10.1074/jbc.M111.274423 en eng American Society for Biochemistry and Molecular Biology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3207396 http://www.ncbi.nlm.nih.gov/pubmed/21900238 http://dx.doi.org/10.1074/jbc.M111.274423 © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Protein Structure and Folding Text 2011 ftpubmed https://doi.org/10.1074/jbc.M111.274423 2013-09-03T22:02:29Z Background: Cold-adapted enzymes remain catalytically active at low temperatures. Text Antarc* Antarctic PubMed Central (PMC) Antarctic Journal of Biological Chemistry 286 44 38348 38355
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Protein Structure and Folding
spellingShingle Protein Structure and Folding
Cipolla, Alexandre
D'Amico, Salvino
Barumandzadeh, Roya
Matagne, André
Feller, Georges
Stepwise Adaptations to Low Temperature as Revealed by Multiple Mutants of Psychrophilic α-Amylase from Antarctic Bacterium*
topic_facet Protein Structure and Folding
description Background: Cold-adapted enzymes remain catalytically active at low temperatures.
format Text
author Cipolla, Alexandre
D'Amico, Salvino
Barumandzadeh, Roya
Matagne, André
Feller, Georges
author_facet Cipolla, Alexandre
D'Amico, Salvino
Barumandzadeh, Roya
Matagne, André
Feller, Georges
author_sort Cipolla, Alexandre
title Stepwise Adaptations to Low Temperature as Revealed by Multiple Mutants of Psychrophilic α-Amylase from Antarctic Bacterium*
title_short Stepwise Adaptations to Low Temperature as Revealed by Multiple Mutants of Psychrophilic α-Amylase from Antarctic Bacterium*
title_full Stepwise Adaptations to Low Temperature as Revealed by Multiple Mutants of Psychrophilic α-Amylase from Antarctic Bacterium*
title_fullStr Stepwise Adaptations to Low Temperature as Revealed by Multiple Mutants of Psychrophilic α-Amylase from Antarctic Bacterium*
title_full_unstemmed Stepwise Adaptations to Low Temperature as Revealed by Multiple Mutants of Psychrophilic α-Amylase from Antarctic Bacterium*
title_sort stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic α-amylase from antarctic bacterium*
publisher American Society for Biochemistry and Molecular Biology
publishDate 2011
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3207396
http://www.ncbi.nlm.nih.gov/pubmed/21900238
https://doi.org/10.1074/jbc.M111.274423
geographic Antarctic
geographic_facet Antarctic
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3207396
http://www.ncbi.nlm.nih.gov/pubmed/21900238
http://dx.doi.org/10.1074/jbc.M111.274423
op_rights © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
op_doi https://doi.org/10.1074/jbc.M111.274423
container_title Journal of Biological Chemistry
container_volume 286
container_issue 44
container_start_page 38348
op_container_end_page 38355
_version_ 1766248427530747904

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