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
Bacterial degradation of xenobiotic compounds: evolution and distribution of novel enzyme activities
TL;DR: A broad range of dehalogenases, which can be classified in different protein superfamilies and have fundamentally different catalytic mechanisms, have been found in isolated bacterial cultures and genomic databases as mentioned in this paper.
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Halohydrin Dehalogenases Are Structurally and Mechanistically Related to Short-Chain Dehydrogenases/Reductases
Johan E. T. van Hylckama Vlieg,Lixia Tang,Jeffrey H. Lutje Spelberg,Tim Smilda,Gerrit J. Poelarends,Tjibbe Bosma,Annet E. J. van Merode,Marco W. Fraaije,Dick B. Janssen +8 more
TL;DR: A site-directed mutagenesis study, with HheC as a model enzyme, supports a mechanism for halohydrin dehalogenases in which the conserved Tyr145 acts as a catalytic base and Ser132 is involved in substrate binding, since it does not involve a covalent enzyme-substrate intermediate.
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The lactococcal lmrp gene encodes a proton motive force-dependent drug transporter
Henk Bolhuis,Gerrit J. Poelarends,HW van Veen,Berend Poolman,Arnold J. M. Driessen,Wil N. Konings +5 more
TL;DR: Results indicate that in the absence of the functional drug-proton antiporter LmrP, L. lactis is able to overexpress another, ATP-dependent, drug extrusion system, and substantiate earlier studies on the isolation and characterization of drug-resistant mutants of L. latis.
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Proton motive force-driven and ATP-dependent drug extrusion systems in multidrug-resistant Lactococcus lactis.
Henk Bolhuis,Douwe Molenaar,Gerrit J. Poelarends,HW van Veen,Berend Poolman,Arnold J. M. Driessen,Wil N. Konings +6 more
TL;DR: The partial inhibition of ethidium efflux by ortho-vanadate and nigericin in the DauR and RhoR strains suggest that a proton motive force-dependent and an ATP-dependent system are expressed simultaneously, the first report of an ATP -dependent transport system in prokaryotes which confers multidrug resistance to the organism.
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Degradation of 1,3-dichloropropene by pseudomonas cichorii 170.
TL;DR: The haloalkane dehalogenase gene, which is involved in the conversion of 1,3-dichloropropene to 3-chloroallyl alcohol, was cloned and sequenced, and this gene turned out to be identical to the previously studied dhaA gene of the gram-positive bacterium Rhodococcus rhodochrous NCIMB13064.