Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Magnús M, Kristjánsson"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1867:152-162
Cloning into a pET 11a vector, followed by high-level expression of the cold adapted subtilase, VPR, utilizing the rhamnose titratable T7 system of Lemo21, resulted in a dramatic increase of soluble protein compared to the older system used. Expressi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::131aff323d96cd2c46575991bb579c50
https://doi.org/10.1016/j.bbapap.2018.11.010
https://doi.org/10.1016/j.bbapap.2018.11.010
Autor:
Magnús M. Kristjánsson, Sigríður H. Thorbjarnardóttir, Mads Nygaard, Elena Papaleo, Brynjar Ö. Ellertsson, Kristinn R. Óskarsson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1864:1436-1443
Structural comparisons of the cold adapted subtilase VPR and its thermophilic homologue, aqualysin I (AQUI) indicated the presence of additional salt bridges in the latter. Few of those appear to contribute significantly to thermal stability of AQUI.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61e19d2158b6f6f16031f1e7260bf1ff
https://doi.org/10.1016/j.bbapap.2016.07.003
https://doi.org/10.1016/j.bbapap.2016.07.003
Autor:
Sigríður H. Thorbjarnardóttir, Manuela Magnusdottir, Magnús M. Kristjánsson, Gaetano Invernizzi, Elena Papaleo, Lilja B. Jónsdóttir, Brynjar Ö. Ellertsson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844:2174-2181
Differences in salt bridges are believed to be a structural hallmark of homologous enzymes from differently temperature-adapted organisms. Nevertheless, the role of salt bridges on structural stability is still controversial. While it is clear that m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e9d0a44f1f74b00975dff228f6349a2
https://doi.org/10.1016/j.bbapap.2014.08.011
https://doi.org/10.1016/j.bbapap.2014.08.011
Publikováno v:
Protein & Peptide Letters. 18:545-551
Aqualysin I, is a subtilisin-like serine proteinase, from the thermophilic bacterium Thermus aquaticus. It is predicted that the enzyme contains a salt bridge, D17-R259, connecting the N- and C-terminal regions of the enzyme. Previously we reported o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ceb5962c3eed2c73a1da0df53c1ee633
https://doi.org/10.2174/092986611795222759
https://doi.org/10.2174/092986611795222759
Autor:
Sigríður H. Thorbjarnardóttir, Anna Guðný Sigurðardóttir, Karsten Suhre, Magnús M. Kristjánsson, Jóhanna Arnórsdóttir, Guðmundur Eggertsson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794:512-518
Structural comparisons of VPR, a subtilisin-like serine proteinase from a psychrotrophic Vibrio species and a thermophilic homologue, aqualysin I, have led us to hypothesize about the roles of different residues in the temperature adaptation of the e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2544e577343c768b047ba49ffed077a3
https://doi.org/10.1016/j.bbapap.2008.11.018
https://doi.org/10.1016/j.bbapap.2008.11.018
Publikováno v:
FEBS Journal. 272:832-845
The crystal structure of a subtilisin-like serine proteinase from the psychrotrophic marine bacterium, Vibrio sp. PA-44, was solved by means of molecular replacement and refined at 1.84 A. This is the first structure of a cold-adapted subtilase to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::25e6ea155e67761ac0dec7c9fcdcb406
https://doi.org/10.1111/j.1742-4658.2005.04523.x
https://doi.org/10.1111/j.1742-4658.2005.04523.x
Autor:
Sigrídur H. Thorbjarnardóttir, Gudmundur Eggertsson, Magnús M. Kristjánsson, Olafur T. Magnusson, Jóhanna Arnórsdóttir, Rúna B. Smáradóttir
Publikováno v:
European Journal of Biochemistry. 269:5536-5546
The gene encoding a subtilisin-like serine proteinase in the psychrotrophic Vibrio sp. PA44 has been successfully cloned, sequenced and expressed in Escherichia coli. The gene is 1593 basepairs and encodes a precursor protein of 530 amino acid residu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4055f05fb9c0dba1fcb3be8507db4531
https://doi.org/10.1046/j.1432-1033.2002.03259.x
https://doi.org/10.1046/j.1432-1033.2002.03259.x
Autor:
Haflidi M. Gudmundsson, Magnús M. Kristjánsson, Hiroshi Matsuzawa, Gudni A. Alfredsson, Olafur T. Magnusson
Publikováno v:
European Journal of Biochemistry. 260:752-760
An extracellular serine proteinase purified from cultures of a psychrotrophic Vibrio species (strain PA-44) belongs to the proteinase K family of the superfamily of subtilisin-like proteinases. The enzyme is secreted as a 47-kDa protein, but under mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6eba6d62a07deabcf59e7feac742e2d9
https://doi.org/10.1046/j.1432-1327.1999.00205.x
https://doi.org/10.1046/j.1432-1327.1999.00205.x
Autor:
Magnús M. Kristjánsson, Sigríður H. Thorbjarnardóttir, Ásta Rós Sigtryggsdóttir, Elena Papaleo
Publikováno v:
Biochimica et biophysica acta. 1844(4)
The subtilisin-like serine proteinases, VPR, from a psychrotrophic Vibrio species and aqualysin I (AQUI) from the thermophile Thermus aquaticus , are structural homologues, but differ significantly with respect to stability and catalytic properties.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e874aa508b9e220e65d39b327980cdf
https://pubmed.ncbi.nlm.nih.gov/24561657
https://pubmed.ncbi.nlm.nih.gov/24561657
