Purification, Characterization, and Nucleotide Sequence of the Thermolabile Alpha-Amylase from the Antarctic Psychrotroph Alteromonas Haloplanctis A23
peer reviewed The alpha-amylase excreted by the antarctic bacterium Alteromonas haloplanctis was purified and the corresponding amy gene was cloned and sequenced. N- and C-terminal amino acid sequencing were used to establish the primary structure of the mature A. haloplanctis alpha-amylase which is...
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American Society for Biochemistry and Molecular Biology
1992
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ftorbi:oai:orbi.ulg.ac.be:2268/16397 2024-04-21T07:47:57+00:00 Purification, Characterization, and Nucleotide Sequence of the Thermolabile Alpha-Amylase from the Antarctic Psychrotroph Alteromonas Haloplanctis A23 Feller, Georges Lonhienne, T. Deroanne, Christophe Libioulle, Cécile Van Beeumen, J. Gerday, Charles 1992-03-15 https://orbi.uliege.be/handle/2268/16397 https://orbi.uliege.be/bitstream/2268/16397/1/JBC_1992_AHAwt.pdf en eng American Society for Biochemistry and Molecular Biology urn:issn:0021-9258 urn:issn:1083-351X https://orbi.uliege.be/handle/2268/16397 info:hdl:2268/16397 https://orbi.uliege.be/bitstream/2268/16397/1/JBC_1992_AHAwt.pdf scopus-id:2-s2.0-0026673888 info:pmid:1544904 open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess Journal of Biological Chemistry, 267 (8), 5217-21 (1992-03-15) 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 1992 ftorbi 2024-03-27T14:44:37Z peer reviewed The alpha-amylase excreted by the antarctic bacterium Alteromonas haloplanctis was purified and the corresponding amy gene was cloned and sequenced. N- and C-terminal amino acid sequencing were used to establish the primary structure of the mature A. haloplanctis alpha-amylase which is composed of 453 amino acids with a predicted Mr of 49,340 and a pI of 5.5. Three Ca2+ ions are bound per molecule and its activity is modulated by chloride ions. Within the four consensus sequences, Asp-174, Glu-200, and Asp-264 are the proposed catalytic residues. The psychrotrophic A. haloplanctis alpha-amylase is characterized by a high amylolytic activity at low temperatures, a reduced apparent optimal temperature, and typical thermodynamic activation parameters A. haloplanctis alpha-amylase has also a low thermal stability as demonstrated by the temperature effect on both activity and secondary structure. It is suggested that structure flexibility and lower sensitivity of secondary structure to temperature variations in the low temperature range are the main structural adaptations of the psychrotrophic enzyme. The unusual stacking of small amino acids around the catalytic residues is proposed as a factor inducing active site flexibility and concomitant high activity of the enzyme at low temperatures. Article in Journal/Newspaper Antarc* Antarctic University of Liège: ORBi (Open Repository and Bibliography) |
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 Feller, Georges Lonhienne, T. Deroanne, Christophe Libioulle, Cécile Van Beeumen, J. Gerday, Charles Purification, Characterization, and Nucleotide Sequence of the Thermolabile Alpha-Amylase from the Antarctic Psychrotroph Alteromonas Haloplanctis A23 |
topic_facet |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed The alpha-amylase excreted by the antarctic bacterium Alteromonas haloplanctis was purified and the corresponding amy gene was cloned and sequenced. N- and C-terminal amino acid sequencing were used to establish the primary structure of the mature A. haloplanctis alpha-amylase which is composed of 453 amino acids with a predicted Mr of 49,340 and a pI of 5.5. Three Ca2+ ions are bound per molecule and its activity is modulated by chloride ions. Within the four consensus sequences, Asp-174, Glu-200, and Asp-264 are the proposed catalytic residues. The psychrotrophic A. haloplanctis alpha-amylase is characterized by a high amylolytic activity at low temperatures, a reduced apparent optimal temperature, and typical thermodynamic activation parameters A. haloplanctis alpha-amylase has also a low thermal stability as demonstrated by the temperature effect on both activity and secondary structure. It is suggested that structure flexibility and lower sensitivity of secondary structure to temperature variations in the low temperature range are the main structural adaptations of the psychrotrophic enzyme. The unusual stacking of small amino acids around the catalytic residues is proposed as a factor inducing active site flexibility and concomitant high activity of the enzyme at low temperatures. |
format |
Article in Journal/Newspaper |
author |
Feller, Georges Lonhienne, T. Deroanne, Christophe Libioulle, Cécile Van Beeumen, J. Gerday, Charles |
author_facet |
Feller, Georges Lonhienne, T. Deroanne, Christophe Libioulle, Cécile Van Beeumen, J. Gerday, Charles |
author_sort |
Feller, Georges |
title |
Purification, Characterization, and Nucleotide Sequence of the Thermolabile Alpha-Amylase from the Antarctic Psychrotroph Alteromonas Haloplanctis A23 |
title_short |
Purification, Characterization, and Nucleotide Sequence of the Thermolabile Alpha-Amylase from the Antarctic Psychrotroph Alteromonas Haloplanctis A23 |
title_full |
Purification, Characterization, and Nucleotide Sequence of the Thermolabile Alpha-Amylase from the Antarctic Psychrotroph Alteromonas Haloplanctis A23 |
title_fullStr |
Purification, Characterization, and Nucleotide Sequence of the Thermolabile Alpha-Amylase from the Antarctic Psychrotroph Alteromonas Haloplanctis A23 |
title_full_unstemmed |
Purification, Characterization, and Nucleotide Sequence of the Thermolabile Alpha-Amylase from the Antarctic Psychrotroph Alteromonas Haloplanctis A23 |
title_sort |
purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph alteromonas haloplanctis a23 |
publisher |
American Society for Biochemistry and Molecular Biology |
publishDate |
1992 |
url |
https://orbi.uliege.be/handle/2268/16397 https://orbi.uliege.be/bitstream/2268/16397/1/JBC_1992_AHAwt.pdf |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Journal of Biological Chemistry, 267 (8), 5217-21 (1992-03-15) |
op_relation |
urn:issn:0021-9258 urn:issn:1083-351X https://orbi.uliege.be/handle/2268/16397 info:hdl:2268/16397 https://orbi.uliege.be/bitstream/2268/16397/1/JBC_1992_AHAwt.pdf scopus-id:2-s2.0-0026673888 info:pmid:1544904 |
op_rights |
open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess |
_version_ |
1796947621330288640 |