Zobrazeno 1 - 10
of 259
pro vyhledávání: '"Eijsink VGH"'
Autor:
Eva Madland, Kresten Lindorff-Larsen, Yong Wang, Jan Modregger, Finn Lillelund Aachmann, Gaston Courtade, Axel Niebisch, Zarah Forsberg, Eijsink Vgh
Among the extensive repertoire of carbohydrate-active enzymes, lytic polysaccharide monooxygenases (LPMOs) have a key role in recalcitrant biomass degradation. LPMOs are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b730f88b43bcc235563dcd683efd3f82
https://doi.org/10.1101/2021.04.25.441307
https://doi.org/10.1101/2021.04.25.441307
Publikováno v:
Protein Science, 20, 8, pp. 1346-55
Protein Science, 20, 1346-55
Protein Science, 20, 1346-55
Item does not contain fulltext Thermolysin and other secreted broad-specificity proteases, such as subtilisin or alpha-lytic protease, are produced as pre-pro-proteins that stay at least partially unfolded while in the cytosol. After secretion, the p
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 95(5), 2056-2060. NATL ACAD SCIENCES
In recent years, many efforts have been made to isolate enzymes from extremophilic organisms in the hope to unravel the structural basis for hyperstability and to obtain hyperstable biocatalysts. Here we show how a moderately stable enzyme (a thermol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::aaeff11e67f4d4a80a4e025d72df83b3
https://research.rug.nl/en/publications/f27598e0-52d4-4b2e-bddf-64d203d5be95
https://research.rug.nl/en/publications/f27598e0-52d4-4b2e-bddf-64d203d5be95
Autor:
VandenBurg, B, Eijsink, VGH, Vriend, G, Veltman, OR, Venema, G, HopsuHavu, VK, Jarvinen, M, Kirschke, H
Publikováno v:
PROTEOLYSIS IN CELL FUNCTIONS, 120-127
STARTPAGE=120;ENDPAGE=127;TITLE=PROTEOLYSIS IN CELL FUNCTIONS
STARTPAGE=120;ENDPAGE=127;TITLE=PROTEOLYSIS IN CELL FUNCTIONS
Autolytic degradation of Bacillus subtilis thermolysin-like proteinase (TLP-sub) is responsible for the irreversible inactivation of the enzyme at elevated temperatures. Previously, we reported five autolysis sites in B. subtilis neutral protease (Va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::3742668aa42940f800ce44b28dc4be00
https://research.rug.nl/en/publications/b89ffe75-e47d-4541-a921-a91e0119d0d9
https://research.rug.nl/en/publications/b89ffe75-e47d-4541-a921-a91e0119d0d9
Publikováno v:
Microbiology-Uk, 141, 123-131. MAIK NAUKA/INTERPERIODICA/SPRINGER
A gene encoding a chitinase from Serratia marcescens BJL200 was cloned and expressed in Escherichia coli and S. marcescens. Nucleotide sequencing revealed an open reading frame encoding a 55.5 kDa protein of 499 amino acids without a typical signal p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::e6d8667ea87d595115d2ec6feae12bfc
https://research.rug.nl/en/publications/99422a88-0ab5-4273-94c3-83b02e936ed4
https://research.rug.nl/en/publications/99422a88-0ab5-4273-94c3-83b02e936ed4
Publikováno v:
Protein Engineering, 7(3), 425-430
Using genetic techniques the contribution of surface loops to the thermal stability of Bacillus subtilis neutral protease (NP-sub) was studied. Mutations were designed to make the surface of NP-sub more similar to the surface of more thermostable neu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::f6e8ab5de55a9a2eaf5c3a6203ba3e26
https://research.rug.nl/en/publications/540c3769-5528-4380-9e5d-c8c91142adf1
https://research.rug.nl/en/publications/540c3769-5528-4380-9e5d-c8c91142adf1
Publikováno v:
FEBS Letters, 317(1-2), 89-92. Wiley
The thermostability of neutral proteases has been shown to depend on autolysis which presumably occurs in flexible regions of the protein. In an attempt to rigidify such a region in the neutral protease of Bacillus stearothermophilus, residues in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::cf918310991d0321f2807edb7a23ec23
https://research.rug.nl/en/publications/a5ca0028-8caf-460e-83bb-89883a40c35e
https://research.rug.nl/en/publications/a5ca0028-8caf-460e-83bb-89883a40c35e
Autor:
EIJSINK, VGH, VRIEND, G, HARDY, F, VELTMAN, OR, VANDERVINNE, B, VANDENBURG, B, DIJKSTRA, BW, VANDERZEE, [No Value], VENEMA, G, VandenTweel, WJJ, Harder, A, Buitelaar, RM
Publikováno v:
STABILITY AND STABILIZATION OF ENZYMES, 91-99
STARTPAGE=91;ENDPAGE=99;TITLE=STABILITY AND STABILIZATION OF ENZYMES
STARTPAGE=91;ENDPAGE=99;TITLE=STABILITY AND STABILIZATION OF ENZYMES
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::e1a0217a907df1d5d2928eea5af2b36a
https://research.rug.nl/en/publications/31f7c2a1-87ef-4f46-8d2d-b1ddd4adfba2
https://research.rug.nl/en/publications/31f7c2a1-87ef-4f46-8d2d-b1ddd4adfba2
Autor:
EIJSINK, VGH, VRIEND, G, VANDENBURG, B, VANDERZEE, [No Value], VELTMAN, OR, STULP, BK, VENEMA, G
Publikováno v:
Protein Engineering, 5(2), 157-163
A 10 residue beta-hairpin, which is characteristic of thermostable Bacillus neutral proteases, was engineered into the thermolabile neutral protease of Bacillus subtilis. The recipient enzyme remained fully active after introduction of the loop. Howe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::8c66c1f393444cb5c43044ec338b2878
https://research.rug.nl/en/publications/06078fd8-7cf1-4112-897c-47d7a02405df
https://research.rug.nl/en/publications/06078fd8-7cf1-4112-897c-47d7a02405df
Publikováno v:
Protein Engineering, 4(8), 941-945
Using site-directed mutagenesis, Ala166 in the neutral protease of Bacillus stearothermophilus was changed into Ser. Model building and molecular dynamics simulations of the mutant enzyme indicated that the Ser hydroxyl group fits well in a cavity wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::d124d87a38a7daef0cae016248fa4a0e
https://research.rug.nl/en/publications/272cb7ad-7481-47d7-92ea-a70ce34edc4b
https://research.rug.nl/en/publications/272cb7ad-7481-47d7-92ea-a70ce34edc4b