Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Sabine Brinkmann-Chen"'
Autor:
Susanne Bähr, Marc Garcia-Borràs, Dimitris Elias Katsoulis, Frances H. Arnold, John M. Roberts, Kendall N. Houk, Sabine Brinkmann-Chen
Publikováno v:
Angew Chem Int Ed Engl
Angewandte Chemie (International ed. in English), vol 59, iss 36
Angewandte Chemie (International ed. in English), vol 59, iss 36
Compared to the biological world’s rich chemistry for functionalizing carbon, enzymatic transformations of the heavier homologue silicon are rare. We report that a wild-type cytochrome P450 monooxygenase (P450BM3 from Bacillus megaterium, CYP102A1)
Autor:
Philipp Koch, Christina E. Boville, Frances H. Arnold, Sabine Brinkmann-Chen, Remkes A. Scheele, Andrew R. Buller
Publikováno v:
Angewandte Chemie. 130:14980-14984
Noncanonical amino acids (ncAAs) with dual stereocenters at the α and β positions are valuable precursors to natural products and therapeutics. Despite the potential applications of such bioactive β-branched ncAAs, their availability is limited du
Autor:
Sabine Brinkmann-Chen, Javier Murciano-Calles, Frances H. Arnold, Andrew R. Buller, David K. Romney
Publikováno v:
Angewandte Chemie. 128:11749-11753
Naturally occurring enzyme homologs often display highly divergent activity with non-natural substrates. Exploiting this diversity with enzymes engineered for new or altered function, however, is laborious because the engineering must be replicated f
Publikováno v:
Protein Science. 25:1241-1248
The duplication of protein structural domains has been proposed as a common mechanism for the generation of new protein folds. A particularly interesting case is the class II ketol-acid reductoisomerase (KARI), which putatively arose from an ancestra
Publikováno v:
Methods in Molecular Biology ISBN: 9781493972944
The specificity of enzymes for nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) as redox carriers can pose a significant hurdle for metabolic engineering and synthetic biology applications, where switching
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c86ef8e73f740f2bdadfde24292a0d14
https://doi.org/10.1007/978-1-4939-7295-1_2
https://doi.org/10.1007/978-1-4939-7295-1_2
Autor:
Christina E. Boville, Remkes A. Scheele, Philipp Koch, Sabine Brinkmann-Chen, Andrew R. Buller, Frances H. Arnold
Non-canonical amino acids (ncAAs) with dual stereocenters at the α and β positions are valuable precursors to natural products and therapeutics. Despite the potential applications of such bioactive β-branched ncAAs, their availability is limited d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef5994c74a55cf98ae9d967613086f58
https://doi.org/10.26434/chemrxiv.6813446
https://doi.org/10.26434/chemrxiv.6813446
Autor:
Sabine Brinkmann-Chen, Jared A. Wiig, Markus W. Ribbe, Yilin Hu, Andrew R. Buller, Frances H. Arnold, Thomas Spatzal, Oliver Einsle, Jackson K. B. Cahn
Publikováno v:
The Biochemical journal, vol 468, iss 3
Although most sequenced members of the industrially important ketol-acid reductoisomerase (KARI) family are class I enzymes, structural studies to date have focused primarily on the class II KARIs, which arose through domain duplication. In the prese
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1671
The specificity of enzymes for nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) as redox carriers can pose a significant hurdle for metabolic engineering and synthetic biology applications, where switching
Autor:
Ruijie K. Zhang, Sabine Brinkmann-Chen, Christopher K. Prier, Andrew R. Buller, Frances H. Arnold
C–H bonds are ubiquitous structural units of organic molecules. Although these bonds are generally considered to be chemically inert, the recent emergence of methods for C–H functionalization promises to transform the way synthetic chemistry is p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::862272734d50585c19207a4f1a90438b
https://resolver.caltech.edu/CaltechAUTHORS:20170413-120718900
https://resolver.caltech.edu/CaltechAUTHORS:20170413-120718900
Autor:
John A. McIntosh, Tillmann Heinisch, Sabine Brinkmann-Chen, Frances H. Arnold, Sheel C. Dodani, Jackson K. B. Cahn
Publikováno v:
ChemBioChem
A novel cytochrome P450 enzyme TxtE was recently shown to catalyze the direct aromatic nitration of L-tryptophan. This unique chemistry induced us to ask whether TxtE could serve as a platform for engineering new nitration biocatalysts, as a replacem