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Gerrit J. Poelarends

Researcher at University of Groningen

Publications -  154
Citations -  4385

Gerrit J. Poelarends is an academic researcher from University of Groningen. The author has contributed to research in topics: 4-Oxalocrotonate tautomerase & Dehalogenase. The author has an hindex of 36, co-authored 143 publications receiving 3807 citations. Previous affiliations of Gerrit J. Poelarends include University of Texas at Austin.

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Functional and structural characterization of an unusual cofactor-independent oxygenase.

TL;DR: It is shown that an enzyme of unknown activity, RhCC from Rhodococcus jostii RHA1, functions as an oxygenase, using 4-hydroxyphenylenolpyruvate as a substrate, and the structure shows the absence of cofactors, establishing RhCC as a rare example of a redox-metal- and coenzyme-free oxygenase.
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Chemoenzymatic Synthesis of ortho-, meta-, and para-Substituted Derivatives of L-threo-3-Benzyloxyaspartate, An Important Glutamate Transporter Blocker

TL;DR: A new chemical procedure for the synthesis of racemic mixtures of TBOA and its derivatives was explored, which are valuable reference compounds in chiral‐phase HPLC to establish the enantiopurities of the corresponding chemoenzymatically prepared amino acids.
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Multidrug Transporters in Lactic Acid Bacteria

TL;DR: The existing data on Multi-Drug Resistance systems are summarized and recent observations are discussed that suggest the use of new strategies in the ongoing battle against drug-resistant microbial pathogens.
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Unlocking Asymmetric Michael Additions in an Archetypical Class I Aldolase by Directed Evolution

TL;DR: In this article, the 2-deoxy-d-ribose-5-phosphate aldolase (DERA) was designed to catalyze enantioselective Michael addition of nitromethane to α,β-unsaturated aldehydes to yield various pharmaceutically relevant chiral synthons.
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Biocatalytic Enantioselective Hydroaminations for Production of N-Cycloalkyl-Substituted L-Aspartic Acids Using Two C-N Lyases

TL;DR: Given its very broad amine scope, EDDS lyase is an exceptionally powerful synthetic tool that nicely complements the rapidly expanding toolbox of biocatalysts for asymmetric synthesis of noncanonical amino acids.