Works matching AU Dirks‐Hofmeister, Mareike E.
Results: 8
Catechol Oxidase versus Tyrosinase Classification Revisited by Site‐Directed Mutagenesis Studies.
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- Angewandte Chemie, 2019, v. 131, n. 26, p. 8849, doi. 10.1002/ange.201902846
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- Article
A specific amino acid residue in the catalytic site of dandelion polyphenol oxidases acts as 'selector' for substrate specificity.
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- Plant Molecular Biology, 2018, v. 96, n. 1-2, p. 151, doi. 10.1007/s11103-017-0686-5
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- Article
Catechol Oxidase versus Tyrosinase Classification Revisited by Site‐Directed Mutagenesis Studies.
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- Angewandte Chemie International Edition, 2019, v. 58, n. 26, p. 8757, doi. 10.1002/anie.201902846
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- Article
Creating Space for Large Acceptors: Rational Biocatalyst Design for Resveratrol Glycosylation in an Aqueous System.
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- Angewandte Chemie, 2015, v. 127, n. 32, p. 9421, doi. 10.1002/ange.201503605
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- Article
A bottom-up approach towards a bacterial consortium for the biotechnological conversion of chitin to l-lysine.
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- Applied Microbiology & Biotechnology, 2021, v. 105, n. 4, p. 1547, doi. 10.1007/s00253-021-11112-5
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- Article
Structural Diversity in the Dandelion (<i>Taraxacum officinale</i>) Polyphenol Oxidase Family Results in Different Responses to Model Substrates.
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- PLoS ONE, 2014, v. 9, n. 6, p. 1, doi. 10.1371/journal.pone.0099759
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- Article
Parameters That Enhance the Bacterial Expression of Active Plant Polyphenol Oxidases.
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- PLoS ONE, 2013, v. 8, n. 10, p. 1, doi. 10.1371/journal.pone.0077291
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- Article
Creating Space for Large Acceptors: Rational Biocatalyst Design for Resveratrol Glycosylation in an Aqueous System.
- Published in:
- Angewandte Chemie International Edition, 2015, v. 54, n. 32, p. 9289, doi. 10.1002/anie.201503605
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- Article