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Published in 2018 at "ChemCatChem"
DOI: 10.1002/cctc.201701194
Abstract: In the last years, imine reductases (IREDs) have gained importance for the formation of chiral amines by catalyzing asymmetric reductions of imines and chemo‐ and stereoselective reductive aminations. However, all characterized members of this steadily…
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Keywords:
imine reductase;
cofactor specificity;
switching cofactor;
specificity imine ... See more keywords
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Published in 2018 at "Methods in molecular biology"
DOI: 10.1007/978-1-4939-7295-1_2
Abstract: 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 the specificity might…
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Keywords:
enzyme nicotinamide;
cofactor specificity;
biology;
nicotinamide cofactor ... See more keywords
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1
Published in 2022 at "ACS Synthetic Biology"
DOI: 10.1021/acssynbio.2c00315
Abstract: Changing the substrate/cofactor specificity of an enzyme requires multiple mutations at spatially adjacent positions around the substrate pocket. However, this is challenging when solely based on crystal structure information because enzymes undergo dynamic conformational changes…
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Keywords:
logistic regression;
cofactor specificity;
cofactor;
specificity ... See more keywords
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Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-020-16478-0
Abstract: Almost half of all enzymes utilize a metal cofactor. However, the features that dictate the metal utilized by metalloenzymes are poorly understood, limiting our ability to manipulate these enzymes for industrial and health-associated applications. The…
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Keywords:
cofactor specificity;
evolutionary path;
metal;
metal specificity ... See more keywords