Publications since 2011 have been indexed by SCOPUS. Earlier publications (authored as "Anett Kirschner", name at birth, indicated with *) are listed here. A combined citation analysis is available via SCOPUS but requires login.
[63] Kaspar F, Eilert L, Staar S, Oung SW, Wolter M, Ganskow CSG, Kemper S, Klahn P, Jacob CR, Blankenfeldt W, Schallmey A. Biocatalytic ether lipid synthesis by an archaeal glycerolprenylase. Angew Chem Int Ed 2024, e202412597. doi: 10.1002/anie.202412597
[62] Staar M, Ahlborn L, Estévez-Gay M, Pallasch K, Osuna S, Schallmey A. A dynamic loop in halohydrin dehalogenase HheG regulates activity and enantioselectivity in epoxide ring opening. ACS Catalysis 2024;14:15976-15987. doi: 10.1021/acscatal.4c04815
[61] Staar S, Estévez-Gay M, Kaspar F, Osuna S, Schallmey A. Engineering of conserved sequence motif 1 residues in halohydrin dehalogenase HheC simultaneously enhances activity, stability and enantioselectivity. In revision. doi: chemrxiv-2024-cw4cm
[60] Schallmey A. Bioinformatic Methods for Enzyme Identification. In: Jaeger, KE., Liese, A., Syldatk, C. (eds) Introduction to Enzyme Technology. Learning Materials in Biosciences. Springer, Cham; 2024:147-164. ISBN: 978-3-031-42999-6 doi: 10.1007/978-3-031-42999-6_7
[59] Christ HA., Daniel NP, Solarczek J, Fresenborg LS, Schallmey A, Menzel H. Application of electrospun chitosan-based nanofibers as immobilization matrix for biomolecules. Appl Microbiol Biotechnol 2023;107:7071-7087. doi: 10.1007/s00253-023-12777-w
[58] Staar M, Schallmey A. Performance of cross-linked enzyme crystals of engineered halohydrin dehalogenase HheG in different chemical reactor systems. Biotechnol Bioeng 2023;120:3210-3223. doi: 10.1002/bit.28528
[57] Kaspar F, Brandt F, Westarp S, Eilert L, Kemper S, Kurreck A, Neubauer P, Jacob CR, Schallmey A. Biased borate esterification during nucleoside phosphorylase-catalyzed reactions: Apparent equilibrium shifts and kinetic implications. Angew Chem Int Ed 2023;62:e202218492 (Angew Chem 2023;135: e202218492). doi: 10.1002/anie.202218492
[56] Staar M, Staar S, Schallmey A. Crystal contact engineering for enhanced cross-linking efficiency of HheG crystals. Catalysts 2022;12:1553. doi: 10.3390/catal12121553
[55] Bassoli S, Schallmey A, Oble J, Poli G, Pradal A. Short hydroacylation-based synthesis of four aryl-3-hydroxypropanones, predictable biomass-derived C9 platform molecules. Catal Res 2022;2:13. doi: 10.21926/cr.2204036
[54] Solarczek J, Kaspar F, Bauer P, Schallmey A. G-type halohydrin dehalogenases catalyze ring opening reactions of cyclic epoxides with diverse anionic nucleophiles. Chem Eur J 2022;28:e202202343. doi: 10.1002/chem.202202343
[53] Kaspar F, Schallmey A. Chemo-enzymatic synthesis of natural products and their analogs. Curr Opin Biotechnol 2022;77:102759. doi: 10.1016/j.copbio.2022.102759
[52] Mascia F, Pereira SB, Pacheco CC, Oliveira P, Solarczek J, Schallmey A, Kourist R, Alphand V, Tamagnini P. Light-driven hydroxylation of testosterone by Synechocystis sp. PCC 6803 expressing the heterologous CYP450 monooxygenase CYP110D1. Green Chem 2022;24:6156-6167. doi: 10.1039.D1GC04714K
[51] Kaspar F, Ganskow CSG, Eilert L, Klahn P, Schallmey A. Alternative assay reagents for UV-spectroscopic detection of (pyro-)phosphate with the PUB module. Anal Chem 2022;94:8132-8135. doi: 10.1021/acs.analchem.2c01404
[50] Staar M, Henke S, Blankenfeldt W, Schallmey A. Biocatalytically active and stable cross-linked enzyme crystals of halohydrin dehalogenase HheG by protein engineering. ChemCatChem 2022;14:e20220014. doi: 10.1002/cctc.202200145
[49] Eilert L, Schallmey A, Kaspar F. UV-Spectroscopic detection of (pyro-)phosphate with the PUB module. Anal Chem 2022;94:3432–3435. doi: 10.1021/acs.analchem.1c05356
[48] Xiang L, Kaspar F, Schallmey A, Constantinou I. Two-phase biocatalysis in microfluidic droplets. Biosensors 2021;11:407. doi:10.3390/bios11110407
[47] Calderini E, Süss P, Hollmann F, Wardenga R, Schallmey A. Two (chemo-)enzymatic cascades for the production of opposite enantiomers of chiral azidoalcohols. Catalysts 2021;11:982. doi:10.3390/catal11080982
[46] Kaspar F, Seeger M, Westarp S, Köllmann C, Lehmann A, Pausch P, Kemper S, Neubauer P, Bange G, Schallmey A, Werz DB, Kurreck A. Diversification of 4ʹ-methylated nucleosides by nucleoside phosphorylases. ACS Catal 2021;11:10830-10835. doi:10.1021/acscatal.1c02589
[45] Kubiak M, Staar M, Kampen I, Schallmey A, Schilde C. The depth-dependent mechanical behavior of anisotropic native and cross-linked HheG enzyme crystals. Crystals 2021;11:718. doi:10.3390/cryst11070718
[44] Martínez-Montero L, Tischler D, Süss P, Schallmey A, Franssen MCR, Hollmann F, Paul CE. Asymmetric azidohydroxylation of styrene derivatives mediated by a biomimetic styrene monooxygenase enzymatic cascade. Catal Sci Technol 2021;11:5077-5085. doi:10.1039/D1CY00855B
[43] Wessel J, Petrillo G, Estevez-Gay M, Bosch Reñe S, Seeger M, Dijkman W, Iglesias-Fernández J, Hidalgo A, Usón I, Osuna S, Schallmey A. Insight into the molecular determinants of thermal stability in halohydrin dehalogenase HheD2. FEBS J 2021;288:4683-4701. doi:10.1111/febs.15777
[42] Schmidt S, Schallmey A, Kourist R. Multi-enzymatic cascades in vitro. In: Kara S, Rudroff F (eds). Enzyme Cascade Design and Modelling. Cham (CH): Springer; 2021:31-48. doi:10.1007/978-3-030-65718-5_3 ISBN:978-3-030-65717-8
[41] Bracco P, Wijma HJ, Nicolai B, Rodriguez Buitrago JA, Klünemann T, Vila A, Schrepfer P, Blankenfeldt W, Janssen DB and Schallmey A. CYP154C5 regioselectivity in steroid hydroxylation explored by substrate modifications and protein engineering. ChemBioChem 2021;22:1099-1110. doi:10.1002/cbic.202000735
[40] Rodriguez Buitrago JA, Klünemann T, Blankenfeldt W and Schallmey A. Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca. Acta Crystallogr Sect F Struct Biol Cryst Commun 2020;76:334-340. doi: 10.1107/S2053230X2000922X
[39] Voß H, Heck CA, Schallmey M, Schallmey A. Database mining for novel bacterial β-etherases, glutathione-dependent lignin-degrading enzymes. Appl Environ Microbiol 2020;86:e02026-19. doi: 10.1128/AEM.02026-19
[38] Leemans L, Walter MD, Hollmann F, Schallmey A, van Langen LM. Multi-catalytic route for the synthesis of (S)-tembamide. Catalysts 2019;9:822. doi: 10.3390/catal9100822
[37] Leemans L, van Langen L, Hollmann F, Schallmey A. Bi-enzymatic cascade for the synthesis of an optically active O-benzoyl cyanohydrin. Catalysts 2019;9:522. doi: 10.3390/catal9060522
[36] Islam MT, Hussain HI, Russo R, Chambery A, Amoresano A, Schallmey A, Oßwald W, Nadiminti PP, Cahill DM. Functional analysis of elicitins and identification of cell wall proteins in Phytophthora cinnamomi. Physiol Mol Plant Pathol 2019;107:21-32. doi: 10.1016/j.pmpp.2019.04.003
[35] Solarczek J, Klünemann T, Brandt F, Schrepfer P, Wolter M, Jacob CR, Blankenfeldt W, Schallmey A. Position 123 of halohydrin dehalogenase HheG plays an important role in stability, activity, and enantioselectivity. Sci Rep 2019;9:5106. doi: 10.1038/s41598-019-41498-2
[34] Calderini E, Wessel J, Süss P, Schrepfer P, Wardenga R, Schallmey A. Selective ring-opening of di-substituted epoxides catalysed by halohydrin dehalogenases. ChemCatChem 2019;11:2099-2106. doi: 10.1002/cctc.201900103
[33] Husarcikova J, Schallmey A. Whole-cell cascade for the preparation of enantiopure beta-O-4 aryl ether compounds with glutathione recycling. J Biotechnol 2019;293:1-7. doi: 10.1016/j.jbiotec.2019.01.002
[32] Schallmey A. Bioinformatische Methoden zur Enzymidentifizierung. In: Jaeger KE, Liese A, Syldatk C (eds). Einführung in die Enzymtechnologie. Berlin, Heidelberg (DE): Springer Spektrum; 2018:125-140. ISBN: 978-3-662-57619-9 doi: 10.1007/978-3-662-57619-9_7
[31] Kubiak M, Solarczek J, Kampen I, Schallmey A, Kwade A, Schilde C. Micromechanics of anisotropic cross-linked enzyme crystals. Cryst Growth Des 2018;18:5885-5895. doi: 10.1021/acs.cgd.8b00637
[30] Husarcikova J, Voß H, Dominguez de Maria P, Schallmey A. Microbial β-etherases and glutathione lyases for lignin valorisation in biorefineries: current state and future perspectives. Appl Microbiol Biotechnol 2018;102:5391-5401. doi: 10.1007/s00253-018-9040-3
[29] Koopmeiners J, Diederich C, Solarczek J, Voß H, Mayer J, Blankenfeldt W, Schallmey A. HheG, a halohydrin dehalogenase with activity on cyclic epoxides. ACS Catal 2017;7:6877-6886. doi: 10.1021/acscatal.7b01854
[28] Picart P, Liu L, Grande PM, Anders N, Zhu L, Klankermayer J, Leitner W, Dominguez de Maria P, Schwaneberg U, Schallmey A. Multi-step biocatalytic depolymerization of lignin. Appl Microbiol Biotechnol 2017;101:6277-6287. doi: 10.1007/s00253-017-8360-z
[27] Schallmey A, Schallmey M. Recent advances on halohydrin dehalogenases - from enzyme identification to novel biocatalytic applications. Appl Microbiol Biotechnol 2016;100:7827-7839. doi: 10.1007/s00253-016-7750-y
[26] Koopmeiners J, Halmschlag B, Schallmey M, Schallmey A. Biochemical and biocatalytic characterization of 17 novel halohydrin dehalogenases. Appl Microbiol Biotechnol 2016;100:7517-7527. doi: 10.1007/s00253-016-7493-9
[25] Picart P, Wiermans L, Perez-Sanchez M, Grande PM, Schallmey A, Dominguez de Maria P. Assessing lignin types to screen novel biomass-degrading microbial strains: Synthetic lignin as useful carbon source. ACS Sustain Chem Eng 2016;4:651-655. doi: 10.1021/acssuschemeng.5b00961
[24] Schallmey A. Enzymatische Ligninverwertung durch bakterielle β-Etherasen. BIOspektrum 2015;21:487-489. doi: 10.1007/s12268-015-0605-8
[23] Picart P, Dominguez de Maria P, Schallmey A. From gene to biorefinery: Microbial β-etherases as promising biocatalysts for lignin valorization. Front Microbiol 2015;6:916. doi: 10.3389/fmicb.2015.00916
[22] Picart P, Sevenich M, Dominguez de Maria P, Schallmey A. Exploring glutathione lyases as biocatalysts: Paving the way for enzymatic lignin depolymerization and future stereoselective applications. Green Chem 2015;17:4931-4940. doi: 10.1039/C5GC01078K
[21] Schallmey M, Koopmeiners J, Wells E, Wardenga R, Schallmey A. Expanding the halohydrin dehalogenase enzyme family: Identification of novel enzymes by database mining. Appl Environ Microb 2014;80:7303-7315. doi: 10.1128/AEM.01985-14
[20] Herzog K, Bracco P, Onoda A, Hayashi T, Hoffmann K, Schallmey A. Enzyme-substrate complex structures of CYP154C5 shed light on its mode of highly selective steroid hydroxylation. Acta Crystallogr D Biol Crystallogr 2014;D70:2875-2889. doi: 10.1107/S1399004714019129
[19] Picart P, Müller C, Mottweiler J, Wiermans L, Bolm C, Dominguez de Maria P, Schallmey, A. From gene towards selective biomass valorization: Novel bacterial beta-etherases with catalytic activity on lignin-like polymers. ChemSusChem 2014;7:3164-3171. doi: 10.1002/cssc.201402465
[18] Wiermanns L, Hofzumahaus S, Schotten C, Weigand L, Schallmey M, Schallmey A, Dominguez de Maria P. Transesterifications and peracid-assisted oxidations in aqueous media catalyzed by Mycobacterium smegmatis acyl transferase. ChemCatChem 2013;5:3719-3724. doi: 10.1002/cctc.201300683
[17] Schallmey A, Schallmey M, Wardenga R. Identifikation neuartiger Halohydrin-Dehalogenasen. BIOspektrum 2013;19:816-817. doi: 10.1007/s12268-013-0394-x
[16] Bracco P, Janssen DB, Schallmey A. Selective steroid oxyfunctionalisation by CYP154C5, a bacterial cytochrome P450. Microb Cell Fact 2013;12:95. doi: 10.1186/1475-2859-12-95
[15] Schallmey A, Dominguez de Maria P, Bracco P. Biocatalytic asymmetric oxidations in stereoselective synthesis. In: Andrushko V, Andrushko N (eds). Stereoselective Synthesis of Drugs & Natural Products. Hoboken (NJ): Wiley-Blackwell; 2013:1089-1114. ISBN: 978-1-118-03217-6 doi: 10.1002/9781118596784.ssd036
[14] Hofzumahaus S, Schallmey A. Escherichia coli-based expression system for the heterologous expression and purification of the elicitin beta-cinnamomin from Phytophthora cinnamomi. Protein Expr Purif 2013;90117-123. doi: 10.1016/j.pep.2013.05.010
[13] Hollmann F, Arends IWCE, Buehler K, Schallmey A, Bühler, B. Enzyme-mediated oxidations for the chemist. Green Chem 2011;13:226-265. doi: 10.1039/C0GC00595A
[12] Schallmey A, den Besten G, Teune IGP, Kembaren RF, Janssen DB. Characterization of cytochrome P450 monooxygenase CYP154H1 from the thermophilic soil bacterium Thermobifida fusca. Appl Microbiol Biotechnol 2011;89:1475-1485. doi: 10.1007/s00253-010-2965-9
[11] *Kirschner A, Bornscheuer UT. Enantioselective kinetic resolution of racemic 3-phenylbutan-2-one using a Baeyer-Villiger monooxygenase. In: Whittall J, Sutton P (eds). Practical Methods for Biocatalysis and Biotransformations. Chichester (UK): John Wiley & Sons; 2009:137-140. ISBN: 978-0-470-51927-1 doi: 10.1002/9780470748589.ch11
[10] *Kirschner A, Bornscheuer UT. Baeyer-Villiger monooxygenases in organic synthesis. In: Anastas PT, Crabtree RH (eds). Handbook of Green Chemistry - Green Catalysis, Vol. 3: Biocatalysis. Weinheim (Germany): Wiley-VCH; 2009:115-149. ISBN: 978-3-527-32498-9 doi: 10.1002/9783527628698
[9] *Kirschner A, Bornscheuer UT. Directed evolution of a Baeyer-Villiger monooxygenase to enhance enantioselectivity. Appl Microbiol Biotechnol 2008;81:465-472. doi: 10.1007/s00253-008-1646-4
[8] Völker A, *Kirschner A, Bornscheuer UT, Altenbuchner J. Functional expression, purification and characterization of the recombinant Baeyer-Villiger monooxygenase MekA from Pseudomonas veronii MEK700. Appl Microbiol Biotechnol 2008;77:1251-1260. doi: 10.1007/s00253-007-1264-6
[7] Rehdorf J, *Kirschner A, Bornscheuer UT. Cloning, expression and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440. Biotechnol Lett 2007;29:1393-1398. doi: 10.1007/s10529-007-9401-y
[6] Geitner K, *Kirschner A, Rehdorf J, Schmidt M, Mihovilovic MD, Bornscheuer UT. Enantioselective kinetic resolution of 3-phenyl-2-ketones using Baeyer-Villiger monooxygenases. Tetrahedron Asymmetry 2007;18:892-895. doi: 10.1016/j.tetasy.2007.03.025
[5] *Kirschner A, Altenbuchner J, Bornscheuer UT. Design of a secondary alcohol degradation pathway from Pseudomonas fluorescens DSM 50106 in an engineered Escherichia coli. Appl Microbiol Biotechnol 2007;75:1095-1101. doi: 10.1007/s00253-007-0902-3
[4] *Kirschner A, Altenbuchner J, Bornscheuer UT. Cloning, expression and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas fluorescens DSM 50106 in E. coli. Appl Microbiol Biotechnol 2007;73:1065-1072. doi: 10.1007/s00253-006-0556-6
[3] *Kirschner A, Bornscheuer UT. Kinetic resolution of 4-hydroxy-2-ketones catalyzed by a Baeyer-Villiger monooxygenase. Angew Chem Int Ed 2006;45:7004-7006. doi: 10.1002/anie.200602986
[2] Strübing D, *Kirschner A, Neumann H, Hübner S, Klaus S, Bornscheuer UT, Beller M. Synthesis of enantiomerically pure cyclohex-2-en-1-ols: Development of novel multicomponent reactions. Chem Eur J 2005;11:4210-4218. doi: 10.1002/chem.200401258
[1] *Kirschner A, Langer P, Bornscheuer UT. Lipase-catalyzed highly enantioselective kinetic resolution of racemic alpha-hydroxy butenolides. Tetrahedron Asymmetry 2004;15:2871-2874. doi: 10.1016/j.tetasy.2004.06.047