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
Alteration of the Diastereoselectivity of 3-Methylaspartate Ammonia Lyase by Using Structure-Based Mutagenesis
Hans Raj,Barbara Weiner,Vinod Puthan Veetil,Carlos R. Reis,Wim J. Quax,Dick B. Janssen,Ben L. Feringa,Gerrit J. Poelarends +7 more
TL;DR: The 1H NMR spectra of the amination and deamination reactions catalyzed by the mutant enzymes K331A, H194A, and Q329A showed that these mutants have strongly enhanced diastereoselectivities.
Journal ArticleDOI
Recent Advances in the Study of Enzyme Promiscuity in the Tautomerase Superfamily
TL;DR: Recent advances in the study of enzyme promiscuity in the tautomerase superfamily are discussed.
Crystal Structures of Native and Inactivated cis-3-Chloroacrylic Acid Dehalogenase STRUCTURALBASISFORSUBSTRATESPECIFICITYANDINACTIVATIONBY (R)-OXIRANE-2-CARBOXYLATE *
Paola Bazzacco,Gerrit J. Poelarends,William H. Johnson,Yoon Jae Kim,Elizabeth A. Burks,Andy-Mark W. H. Thunnissen,Christian P. Whitman,Bauke W. Dijkstra +7 more
Abstract: The bacterial degradation pathways for the nematocide 1,3-dichloropropene rely on hydrolytic dehalogenation reactions catalyzed by cis- and trans-3-chloroacrylic acid dehalogenases (cis-CaaD and CaaD, respectively). X-ray crystal structures of native cis-CaaD and cis-CaaD inactivated by (R)-oxirane-2-carboxylate were elucidated. They locate four known catalytic residues (Pro-1, Arg-70, Arg-73, and Glu-114) and two previously unknown, potential catalytic residues (His-28 and Tyr-103′). The Y103F and H28A mutants of these latter two residues displayed reductions in cis-CaaD activity confirming their importance in catalysis. The structure of the inactivated enzyme shows covalent modification of the Pro-1 nitrogen atom by (R)-2-hydroxypropanoate at the C3 position. The interactions in the complex implicate Arg-70 or a water molecule bound to Arg-70 as the proton donor for the epoxide ring-opening reaction and Arg-73 and His-28 as primary binding contacts for the carboxylate group. This proposed binding mode places the (R)-enantiomer, but not the (S)-enantiomer, in position to covalently modify Pro-1. The absence of His-28 (or an equivalent) in CaaD could account for the fact that CaaD is not inactivated by either enantiomer. The cis-CaaD structures support a mechanism in which Glu-114 and Tyr-103′ activate a water molecule for addition to C3 of the substrate and His-28, Arg-70, and Arg-73 interact with the C1 carboxylate group to assist in substrate binding and polarization. Pro-1 provides a proton at C2. The involvement of His-28 and Tyr-103′ distinguishes the cis-CaaD mechanism from the otherwise parallel CaaD mechanism. The two mechanisms probably evolved independently as the result of an early gene duplication of a common ancestor.
Journal ArticleDOI
Enhancement of the Promiscuous Aldolase and Dehydration Activities of 4-Oxalocrotonate Tautomerase by Protein Engineering
TL;DR: Mechanism-inspired engineering provided an active site mutant (F50A) with strongly enhanced aldol condensation activity and the resulting compound yielded cinnamaldehyde as the final product.
MonographDOI
Biocatalysis in Organic Synthesis
Kurt Faber,Wolf-Dieter Fessner,Nicholas J. Turner,S. K. Au,Sebastian Bartsch,D. Beecher,A. Boffi,A. S. Bommarius,A. Bonamore,G. Brown,Eduardo Busto,P. Clapés,Eva-Maria Fischereder,C. S. Fuchs,Edzard M. Geertsema,A. Glieder,Mandana Gruber-Khadjawi,Mélanie Hall,Ulf Hanefeld,S. Hussain,A. Ilari,Dick B. Janssen,Goran N. Kaluđerović,Wolfgang Kroutil,A. S. Lamm,F. Leipold,Ross Lewin,A. T. Li,Zhi Li,M. Majerić Elenkov,Jason Micklefield,T. S. Moody,S. Mix,Michael Müller,Gerrit J. Poelarends,Martina Pohl,Desiree Pressnitz,Verena Resch,Nina Richter,J. P. N. Rosazza,H. F. Schreckenbach,R. C. Simon,Kerstin Steiner,Wiktor Szymanski,Mark L. Thompson,P. Venkitasubramanian,A. Vogel,Cindy Wechsler,Ludger A. Wessjohann,R. Wohlgemuth +49 more