G
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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Journal ArticleDOI
Structural and functional characterization of a macrophage migration inhibitory factor homologue from the marine cyanobacterium Prochlorococcus marinus .
Anna A. Wasiel,Henriëtte J. Rozeboom,Doreen Hauke,Bert-Jan Baas,Ellen Zandvoort,Wim J. Quax,Andy-Mark W. H. Thunnissen,Gerrit J. Poelarends +7 more
TL;DR: The shared tautomerase activities and the conservation of the beta-alpha-beta structural fold and key functional groups suggest that eukaryotic MIFs and cyanobacterial PmMIF are related by divergent evolution from a common ancestor.
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Enhancement of the enantioselectivity of carboxylesterase A by structure-based mutagenesis
Luis F. Godinho,Carlos R. Reis,Henriëtte J. Rozeboom,Frank J. Dekker,Bauke W. Dijkstra,Gerrit J. Poelarends,Wim J. Quax +6 more
TL;DR: The importance of residues at positions 166 and 182 for the enantioselectivity of CesA is demonstrated, and may contribute to the development of efficient biocatalysts.
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Enantiocomplementary Epoxidation Reactions Catalyzed by an Engineered Cofactor‐Independent Non‐natural Peroxygenase
Guangcai Xu,Michele Crotti,Thangavelu Saravanan,Thangavelu Saravanan,Kim M. Kataja,Gerrit J. Poelarends +5 more
TL;DR: The engineering of an unusual cofactor‐independent peroxygenase based on a promiscuous tautomerase that accepts different hydroperoxides to accomplish enantiocomplementary epoxidations of various α,β‐unsaturated aldehydes (citral and substituted cinnamaldehydes) is reported.
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A three-dimensional model for the substrate binding domain of the multidrug ATP binding cassette transporter LmrA.
Gerhard F. Ecker,Karin Pleban,Stephan Kopp,Edina Csaszar,Gerrit J. Poelarends,M Putman,Dominik Kaiser,Wil N. Konings,Peter Chiba +8 more
TL;DR: Inverse changes in the reactivity of TM segments 5 and 6 suggest that substrate binding and release involves a repositioning of these helices during the catalytic cycle, suggesting substrate-binding at the monomer/monomer interface.