Zobrazeno 1 - 10
of 88
pro vyhledávání: '"A. J. Wijma"'
Autor:
Guang Yang, Ognjen Pećanac, Hein J. Wijma, Henriëtte J. Rozeboom, Gonzalo de Gonzalo, Marco W. Fraaije, Maria Laura Mascotti
Publikováno v:
Cell Reports, Vol 43, Iss 5, Pp 114130- (2024)
Summary: Enzymes are crucial for the emergence and sustenance of life on earth. How they became catalytically active during their evolution is still an open question. Two opposite explanations are plausible: acquiring a mechanism in a series of discr
Externí odkaz:
https://doaj.org/article/feb1f2f992734d9098a5b4944af85d68
Publikováno v:
BBA Advances, Vol 4, Iss , Pp 100097- (2023)
In recent years, studies have shown that a large number of bacteria secrete multi-flavinylated proteins. The exact roles and properties, of these extracellular flavoproteins that contain multiple covalently anchored FMN cofactors, are still largely u
Externí odkaz:
https://doaj.org/article/47bacea9a7bd4e00836afb0201bd2f67
Publikováno v:
Frontiers in Catalysis, Vol 2 (2022)
Protein engineering is a powerful and widely applied tool for tailoring enzyme properties to meet application-specific requirements. An attractive group of biocatalysts are PLP-dependent amine transaminases which are capable of converting prochiral k
Externí odkaz:
https://doaj.org/article/39999081950b43df80b7f653713a0e58
Autor:
Ana Toplak, Eduardo F. Teixeira de Oliveira, Marcel Schmidt, Henriëtte J. Rozeboom, Hein J. Wijma, Linda K.M. Meekels, Rowin de Visser, Dick B. Janssen, Timo Nuijens
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 1277-1287 (2021)
Omniligase-1 is a broadly applicable enzyme for peptide bond formation between an activated acyl donor peptide and a non-protected acyl acceptor peptide. The enzyme is derived from an earlier subtilisin variant called peptiligase by several rounds of
Externí odkaz:
https://doaj.org/article/6a85ba9608194f52a918b9a4228a5b84
Autor:
Francisca Monteiro, Georg Hubmann, Vakil Takhaveev, Silke R Vedelaar, Justin Norder, Johan Hekelaar, Joana Saldida, Athanasios Litsios, Hein J Wijma, Alexander Schmidt, Matthias Heinemann
Publikováno v:
Molecular Systems Biology, Vol 15, Iss 12, Pp 1-20 (2019)
Abstract Metabolic heterogeneity between individual cells of a population harbors significant challenges for fundamental and applied research. Identifying metabolic heterogeneity and investigating its emergence require tools to zoom into metabolism o
Externí odkaz:
https://doaj.org/article/4e0eb7e0221f4bcc8a9bb0a80a89742a
Autor:
C. Najem, A. J. Wijma, M. Meeus, B. Cagnie, F. Ayoubi, J. Van Oosterwijck, K. De Meulemeester, C. P. Van Wilgen
Publikováno v:
Disability and rehabilitation
PurposeThe purpose of this paper was first to gain an in-depth understanding of the barriers and facilitators to implementing the BPS model and pain neuroscience education in the current Lebanese physical therapy health care approach and explore its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4db5d57f5121c3d8acc0a7d968dfc126
https://doi.org/10.1080/09638288.2023.2168076
https://doi.org/10.1080/09638288.2023.2168076
Autor:
Mark A. Ashworth, Elvira Bombino, René M. de Jong, Hein J. Wijma, Dick B. Janssen, Kirsty J. McLean, Andrew W. Munro
Publikováno v:
ACS Catalysis, 12(24), 15028-15044. AMER CHEMICAL SOC
CYP105AS1 is a cytochrome P450 from Amycolatopsis orientalis that catalyzes monooxygenation of compactin to 6-epi-pravastatin. For fermentative production of the cholesterol-lowering drug pravastatin, the stereoselectivity of the enzyme needs to be i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7271774f14d5e45b6c65127419547b8d
https://doi.org/10.1021/acscatal.2c03974
https://doi.org/10.1021/acscatal.2c03974
Publikováno v:
Biotechnology for Biofuels, Vol 11, Iss 1, Pp 1-9 (2018)
Abstract Background HMF oxidase (HMFO) from Methylovorus sp. is a recently characterized flavoprotein oxidase. HMFO is a remarkable enzyme as it is able to oxidize 5-hydroxymethylfurfural (HMF) into 2,5-furandicarboxylic acid (FDCA): a catalytic casc
Externí odkaz:
https://doaj.org/article/cc992bd1f38d41a0b21a69adef4cfd78
Publikováno v:
ChemBioChem, 24(9):e202300032. WILEY-V C H VERLAG GMBH
Whereas directed evolution and rational design by structural inspection are established tools for enzyme redesign, computational methods are less mature but have the potential to predict small sets of mutants with desired properties without laborator
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6acb66ca1c5fa45cc69f53be5d1a9d30
https://doi.org/10.1002/cbic.202300032
https://doi.org/10.1002/cbic.202300032
Autor:
Stefan R. Marsden, Hein J. Wijma, Michael K. F. Mohr, Inês Justo, Peter‐Leon Hagedoorn, Jesper Laustsen, Cy M. Jeffries, Dmitri Svergun, Luuk Mestrom, Duncan G. G. McMillan, Isabel Bento, Ulf Hanefeld
Publikováno v:
Angewandte Chemie / International edition 61(49), e202213338 (2022). doi:10.1002/anie.202213338
Angewandte Chemie (International Edition), 61(49)
Angewandte Chemie-International Edition, 61(49):e202213338. WILEY-V C H VERLAG GMBH
Angewandte Chemie (International Edition), 61(49)
Angewandte Chemie-International Edition, 61(49):e202213338. WILEY-V C H VERLAG GMBH
Angewandte Chemie / International edition 61(49), e202213338 (2022). doi:10.1002/anie.202213338
Regulation of enzyme activity is vital for living organisms. In metalloenzymes, far-reaching rearrangements of the protein scaffold are generally req
Regulation of enzyme activity is vital for living organisms. In metalloenzymes, far-reaching rearrangements of the protein scaffold are generally req
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28c40496c0defb5c566038f72e1882fd
https://doi.org/10.1002/anie.202213338
https://doi.org/10.1002/anie.202213338