Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast
Euphauserase is a brachyurin type digestive enzyme isolated from Antarctic krill. The brachyurins belong to clan SA of the S1 family of serine endopeptidases. In this study, we demonstrate that the precursor form of recombinant euphauserase, termed pro‐r‐euphauserase, can be successfully expressed i...
Published in: | European Journal of Biochemistry |
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Online Access: | http://dx.doi.org/10.1046/j.1432-1327.2000.01273.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.2000.01273.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.2000.01273.x |
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crwiley:10.1046/j.1432-1327.2000.01273.x 2024-06-02T07:58:08+00:00 Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast Kristjánsdóttir, Sigrídur Gudmundsdóttir, Ágústa 2000 http://dx.doi.org/10.1046/j.1432-1327.2000.01273.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.2000.01273.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.2000.01273.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 267, issue 9, page 2632-2639 ISSN 0014-2956 1432-1033 journal-article 2000 crwiley https://doi.org/10.1046/j.1432-1327.2000.01273.x 2024-05-03T10:52:40Z Euphauserase is a brachyurin type digestive enzyme isolated from Antarctic krill. The brachyurins belong to clan SA of the S1 family of serine endopeptidases. In this study, we demonstrate that the precursor form of recombinant euphauserase, termed pro‐r‐euphauserase, can be successfully expressed in Pichia pastoris . The presence of most of the 51‐residue euphauserase propeptide is essential during expression, under the growth conditions of Pichia . The propeptide may be required either for correct folding or processing of the enzyme. Cod trypsin generates a fully active r‐euphauserase from its precursor, which appears to be identical to the native enzyme. The mature r‐euphauserase sequence contains 250 amino‐acid residues including a 13‐residue activation peptide, which seems to be attached to the molecule by a disulfide bond. Euphauserase shares an average sequence identity of 62% with its type I brachyurin analogue, crab collagenase I. However, the identity between these two sequences is much higher in the regions shown to be important for the broad substrate specificity and collagen binding of crab collagenase I. The type I brachyurins share only 30–40% identities with the type II brachyurins and trypsins. The low isoelectric point of euphauserase, with a calculated pI value of 3.9, is typical for the type I brachyurins. Article in Journal/Newspaper Antarc* Antarctic Antarctic Krill Wiley Online Library Antarctic The Antarctic European Journal of Biochemistry 267 9 2632 2639 |
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English |
description |
Euphauserase is a brachyurin type digestive enzyme isolated from Antarctic krill. The brachyurins belong to clan SA of the S1 family of serine endopeptidases. In this study, we demonstrate that the precursor form of recombinant euphauserase, termed pro‐r‐euphauserase, can be successfully expressed in Pichia pastoris . The presence of most of the 51‐residue euphauserase propeptide is essential during expression, under the growth conditions of Pichia . The propeptide may be required either for correct folding or processing of the enzyme. Cod trypsin generates a fully active r‐euphauserase from its precursor, which appears to be identical to the native enzyme. The mature r‐euphauserase sequence contains 250 amino‐acid residues including a 13‐residue activation peptide, which seems to be attached to the molecule by a disulfide bond. Euphauserase shares an average sequence identity of 62% with its type I brachyurin analogue, crab collagenase I. However, the identity between these two sequences is much higher in the regions shown to be important for the broad substrate specificity and collagen binding of crab collagenase I. The type I brachyurins share only 30–40% identities with the type II brachyurins and trypsins. The low isoelectric point of euphauserase, with a calculated pI value of 3.9, is typical for the type I brachyurins. |
format |
Article in Journal/Newspaper |
author |
Kristjánsdóttir, Sigrídur Gudmundsdóttir, Ágústa |
spellingShingle |
Kristjánsdóttir, Sigrídur Gudmundsdóttir, Ágústa Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast |
author_facet |
Kristjánsdóttir, Sigrídur Gudmundsdóttir, Ágústa |
author_sort |
Kristjánsdóttir, Sigrídur |
title |
Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast |
title_short |
Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast |
title_full |
Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast |
title_fullStr |
Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast |
title_full_unstemmed |
Propeptide dependent activation of the Antarctic krill euphauserase precursor produced in yeast |
title_sort |
propeptide dependent activation of the antarctic krill euphauserase precursor produced in yeast |
publisher |
Wiley |
publishDate |
2000 |
url |
http://dx.doi.org/10.1046/j.1432-1327.2000.01273.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.2000.01273.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.2000.01273.x |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Antarctic Krill |
genre_facet |
Antarc* Antarctic Antarctic Krill |
op_source |
European Journal of Biochemistry volume 267, issue 9, page 2632-2639 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1046/j.1432-1327.2000.01273.x |
container_title |
European Journal of Biochemistry |
container_volume |
267 |
container_issue |
9 |
container_start_page |
2632 |
op_container_end_page |
2639 |
_version_ |
1800741410455945216 |