Increasing the thermal stability of euphauserase
A molecular model of Antarctic krill euphauserase based on the known crystal structure of its fiddler crab analog, collagenase I, indicates that the core structure of these enzymes is almost identical. Euphauserase is a cold‐active and thermally sensitive enzyme with a high affinity for Lys, Arg and...
Published in: | European Journal of Biochemistry |
---|---|
Main Authors: | , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2001
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1046/j.1432-1327.2001.01857.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.2001.01857.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.2001.01857.x |
id |
crwiley:10.1046/j.1432-1327.2001.01857.x |
---|---|
record_format |
openpolar |
spelling |
crwiley:10.1046/j.1432-1327.2001.01857.x 2024-06-02T07:57:37+00:00 Increasing the thermal stability of euphauserase A cold‐active and multifunctional serine protease from Antarctic krill Benjamin, David C. Kristjánsdóttir, Sigrídur Gudmundsdóttir, Ágústa 2001 http://dx.doi.org/10.1046/j.1432-1327.2001.01857.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.2001.01857.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.2001.01857.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 268, issue 1, page 127-131 ISSN 0014-2956 1432-1033 journal-article 2001 crwiley https://doi.org/10.1046/j.1432-1327.2001.01857.x 2024-05-03T11:22:27Z A molecular model of Antarctic krill euphauserase based on the known crystal structure of its fiddler crab analog, collagenase I, indicates that the core structure of these enzymes is almost identical. Euphauserase is a cold‐active and thermally sensitive enzyme with a high affinity for Lys, Arg and large hydrophobic amino acids. Residue Phe137 in euphauserase, localized in loop D (autolysis loop), is highly exposed on the surface of the molecule. Therefore, it appeared to be an easy target for autolysis. The broadly specific euphauserase has a low affinity for negatively charged residues. In order to increase the stability of the enzyme, two mutants were created in which residue Phe137 was replaced by a Glu and an Asp residue. Both mutations resulted in increased stability of the recombinant euphauserase towards thermal inactivation. Article in Journal/Newspaper Antarc* Antarctic Antarctic Krill Wiley Online Library Antarctic European Journal of Biochemistry 268 1 127 131 |
institution |
Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
A molecular model of Antarctic krill euphauserase based on the known crystal structure of its fiddler crab analog, collagenase I, indicates that the core structure of these enzymes is almost identical. Euphauserase is a cold‐active and thermally sensitive enzyme with a high affinity for Lys, Arg and large hydrophobic amino acids. Residue Phe137 in euphauserase, localized in loop D (autolysis loop), is highly exposed on the surface of the molecule. Therefore, it appeared to be an easy target for autolysis. The broadly specific euphauserase has a low affinity for negatively charged residues. In order to increase the stability of the enzyme, two mutants were created in which residue Phe137 was replaced by a Glu and an Asp residue. Both mutations resulted in increased stability of the recombinant euphauserase towards thermal inactivation. |
format |
Article in Journal/Newspaper |
author |
Benjamin, David C. Kristjánsdóttir, Sigrídur Gudmundsdóttir, Ágústa |
spellingShingle |
Benjamin, David C. Kristjánsdóttir, Sigrídur Gudmundsdóttir, Ágústa Increasing the thermal stability of euphauserase |
author_facet |
Benjamin, David C. Kristjánsdóttir, Sigrídur Gudmundsdóttir, Ágústa |
author_sort |
Benjamin, David C. |
title |
Increasing the thermal stability of euphauserase |
title_short |
Increasing the thermal stability of euphauserase |
title_full |
Increasing the thermal stability of euphauserase |
title_fullStr |
Increasing the thermal stability of euphauserase |
title_full_unstemmed |
Increasing the thermal stability of euphauserase |
title_sort |
increasing the thermal stability of euphauserase |
publisher |
Wiley |
publishDate |
2001 |
url |
http://dx.doi.org/10.1046/j.1432-1327.2001.01857.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.2001.01857.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.2001.01857.x |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic Antarctic Krill |
genre_facet |
Antarc* Antarctic Antarctic Krill |
op_source |
European Journal of Biochemistry volume 268, issue 1, page 127-131 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1046/j.1432-1327.2001.01857.x |
container_title |
European Journal of Biochemistry |
container_volume |
268 |
container_issue |
1 |
container_start_page |
127 |
op_container_end_page |
131 |
_version_ |
1800740786366578688 |