• A. C. R. Ngo, B. Celebi, S. N. Hermann Hadewig, C. Mügge, D. Tischler Selective Pressure Leads to an Improved Synthetic Consortium Fit for Dye Degradation. Chemosphere (2024)  DOI:10.1016/j.chemosphere.2024.142489
  • F. P. J. Schultes, L. Welter, D. Hufnagel, M. Heghmanns, M. Kasanmascheff, C. Muegge, An Active and Versatile Electron Transport System for Cytochrome P450 Monooxygenases from the Alkane Degrading Organism Acinetobacter Sp. OC4. ChemBioChem (2024)  DOI:10.1002/cbic.202400098
  • B. M. Nestl, B. A. Nebel, V. Resch, M. Schürmann, D. Tischler, The development and opportunities of predictive biotechnology (2024) ChemBioChem. DOI: 10.1002/cbic.202300863
  • A. Maier, T. Knaus, F.G. Mutti, D. Tischler, Unlocking Catalytic Diversity of a Formate Dehydrogenase: Formamide Activity for NADPH Regeneration and Amine Supply for Asymmetric Reductive Amination (2024) ACS Catal. DOI: 10.1021/acscatal.3c05409
  • G. Vasilopoulos, L. Heflik, S. Czolkoss, F. Heinrichs, J. Kleetz, C. Yesilyurt, D. Tischler, P. Westhoff, M. Exterkate, M. Aktas, F. Narberhaus, Characterization of multiple lysophosphatidic acid acyltransferases in the plant pathogen Xanthomonas campestris (2024) FEBS J. DOI: 10.1111/febs.16996
  • S. Schröder, A. Maier, A. Schmidt, C. Mügge, D. Tischler, Enhancing biocatalytical N-N bond formation with the actinobacterial piperazate synthase KtzT (2024) Mol. Catal. DOI: 10.1016/j.mcat.2023.113733
  • C. Mügge, N. Nowak, M. Strack, N. Metzler-Nolte and W. Weigand, Synthetic Approaches towards Peptide-Conjugates of Pt(II) Compounds with an (O,S) Chelating Moiety, European Journal of Inorganic Chemistry (2023) DOI:10.1002/ejic.202300519
  • D. Eggerichs, N. Weindorf, L.M. Mascotti, N. Welzel, M.W. Fraaijs, D. Tischler, Vanillyl alcohol oxidase from Diplodia corticola: Residues Ala420 and Glu466 allow for efficient catalysis of syringyl derivatives (2023) J. Biol. Chem. DOI: 10.1016/j.jbc.2023.104898
  • D. Eggerichs, K. Zilske, D. Tischler, Large Scale Production of Vanillin Using an Eugenol Oxidase from Nocardioides Sp. YR527. Molecular Catalysis (2023).
  • J. Holste, C. Mügge, C. Distler, S. Schulz, The Uropygial Gland of the Great Cormorant (Phalacrocorax Carbo): II. Biochemical Analysis of the Uropygial Secretion. Journal of Ornithology (2023).
  • F.P.J. Schultes, M. Haarmann, D. Tischler, C. Mügge, Primary alcohols as substrates or products in whole-cell biocatalysis: Toxicity for Escherichia coli expression strains (2023) Molecular Catalysis DOI: 10.1016/j.mcat.2023.112979
  • J. Kratky, D. Eggerichs, T. Heine, S. Hofmann, P. Sowa, R.H. Weiße, D. Tischler, N. Sträter,Structural and Mechanistical Studies on Substrate and Stereo Selectivity of the Indole Monooxygenase VpIndA1: New Avenues for Biocatalytic Epoxidations and Sulfoxidations (2023) Angew. Chem. Int. Ed. DOI: 10.1002/anie.202300657
  • V. Petkevičius, J. Vaitekūnas, M. Sadauskas, F.P.J. Schultes, D. Tischler, R. Meškys, The versatility of non-heme diiron monooxygenase PmlABCDEF: a single biocatalyst for a plethora of oxygenation reactions (2022) Catal. Sci. Technol. DOI: 10.1039/d2cy01167k.
  • J. Rolf, A.C.R. Ngo, S. Lütz, D. Tischler, K. Rosenthal, Cell-free protein synthesis for the screening of novel azoreductases and their preferred electron donor (2022) ChemBioChem DOI: 10.1002/cbic.202200121.
  • A.C.R. Ngo, D. Tischler, Microbial degradation of azo dyes: Approaches and prospects for a hazard-free conversion by microorganisms (2022) Int. J. Environ. Res. Public Health DOI: 10.3390/ijerph19084740. 
  • D. Tischler, Buchrezension zu: The Autotrophic Biorefinery (2022) BioSpektrum DOI: 10.1007/s12268-022-1698-5. 
  • A.C.R. Ngo, F.P.J. Schultes, A. Maier, S.N.H. Hadewig, D. Tischler, Improving biocatalytic properties of an azoreductase via the N-terminal fusion of formate dehydrogenase (2022) ChemBioChem DOI: 10.1002/cbic.202100643.
  • A.C.R. Ngo, J. Qi, C. Juric, I. Bento, D. Tischler, (2022) Identification of molecular basis that underlie enzymatic specificity of AzoRo from Rhodococcus opacus 1CP: A potential NADH:quinone oxidoreductase (2022) Arch. Biochem. Biophys. DOI: 10.1016/
  • S. Kumaran, A.C.R. Ngo, F.P.J. Schultes, V.S. Saravanan, D. Tischler, In vitro and in silico analysis of Brilliant Black degradation by Actinobacteria and a Paraburkholderia sp. (2022) Genomics DOI: 10.1016/j.ygeno.2022.01.003.
  • D. Kowalczykiewicz, M. Przypis, L. Mestrom, A. Kumpf, D. Tischler, P.-L. Hagedoorn, U. Hanefeld, A. Jarzębski, K. Szymańska, Engineering of continuous bienzymatic cascade process using monolithic microreactors – in flow synthesis of trehalose (2022) Chem. Eng. J. DOI: 10.1016/j.cej.2021.131439.
  • A.C.R. Ngo, C. Conrad, A.G. Baraibar, A. Matura, K.-H. van Pée, D. Tischler, Characterization of two hydrogen peroxide resistant peroxidases from Rhodococcus opacus 1CP (2021) Appl. Sci. DOI: 10.3390/app11177941.
  • A.C. Lienkamp, J. Burnik, T. Heine, E. Hofmann, D. Tischler, Characterization of the Glutathione S-Transferases Involved in Styrene Degradation in Gordonia rubripertincta CWB2 (2021) Microbiol. Spectr. DOI: 10.1128/Spectrum.00474-21.
  • R. Schwabe, C. Dittrich, J. Kadner, C.H.R. Senges, J.E. Bandow, D. Tischler, M. Schlömann, G. Levicán, O. Wiche, Secondary metabolites released by the rhizosphere bacteria Arthrobacter oxydans and Kocuria rosea enhance plant availability and soil–plant transfer of germanium (Ge) and rare earth elements (REEs) (2021) Chemosphere DOI:10.1016/j.chemosphere.2021.131466.
  • L. Martínez-Montero, D. Tischler, P. Süss, A. Schallmey, M.C.R. Franssen, F. Hollmann, C.E. Paul, Asymmetric azidohydroxylation of styrene derivatives mediated by a biomimetic styrene monooxygenase enzymatic cascade (2021) Catal. Sci. Technol. DOI:10.1039/D1CY00855B.
  • A.C. Lienkamp, M. Haarmann, D. Tischler, Gordonia: versatile actinobacteria for biotechnology (2021) IOP Conf. Ser.: Earth Environ. Sci. DOI:10.1088/1755-1315/689/1/012024.
  • O.Y. Mezenova, D. Tischler, S.V. Agafonova, N.Y. Mezenova, V.V. Volkov, D.A. Baranenko, T. Grimm, S. Riedel, Research and rational use of peptide and lipid compositions obtained by hydrolysis processing of collagen-containing tissues (2021) J. Int. Acad. Refrig. DOI:10.17586/1606-4313-2021-20-1-46-58.
  • A.H.Westphal, D. Tischler, W.J.H. van Berkel, Natural diversity of FAD-dependent 4-hydroxybenzoate hydroxylases (2021) Arch. Biochem. Biophyis. DOI: 10.1016/
  • C.E. Paul, D. Eggerichs, A.H. Westphal, D. Tischler, W.J.H. van Berkel, Flavoprotein monooxygenases: Versatile biocatalysts (2021) Biotechnol. Adv. DOI: 10.1016/j.biotechadv.2021.107712.
  • G. Retamal-Morales, C.H.R. Senges, M. Stapf, A. Olguín, B. Modak, J.E. Bandow, D. Tischler, M. Schlömann, G. Levicán, Isolation and characterization of arsenic-binding siderophores from Rhodococcus erythropolis S43: role of heterobactin B and other heterobactin variants (2021) Appl. Microbiol. Biotechnol. DOI: 10.1007/s00253-021-11123-2
  • M. Hofmann, T. Heine, L. Malik, S. Hofmann, K. Joffroy, C.H.R Senges, J.E Bandow, D. Tischler, Screening for microbial metal-chelating siderophores for the removal of metal Ions from solutions (2021) Microorganisms DOI: 10.3390/microorganisms9010111
  • J. Zimmerling, M. Oelschlägel, C. Großmann, M. Voitel, M. Schlömann, D. Tischler, Biochemical characterization of phenylacetaldehyde dehydrogenases from styrene-degrading soil bacteria (2021) Appl. Biochem. Biotechnol. DOI: 10.1007/s12010-020-03421-8
  • C. Mügge, T. Heine, A.G. Baraibar, W.J.H. van Berkel, C.E. Paul, D. Tischler, Flavin-dependent N-hydroxylating enzymes: distribution and application (2020) Appl. Microbiol. Biotechnol. DOI: 10.1007/s00253-020-10705-w
  • S. Böhmer, C. Marx, A. Gómez-Baraibar, M.M. Nowaczyk, D. Tischler, A. Hemschemeier, T. Happe, Evolutionary diverse Chlamydomonas reinhardtii Old Yellow Enzymes reveal distinctive catalytic properties and potential for whole-cell biotransformations (2020) Algal Res. DOI: 10.1016/j.algal.2020.101970
  • D. Tischler, A perspective on enzyme inhibitors from marine organisms (2020) Mar. Drugs DOI: 10.3390/MD18090431
  • D. Tischler, A. Kumpf, D. Eggerichs, T. Heine, Styrene monooxygenases, indole monooxygenases and related flavoproteins applied in bioremediation and biocatalysis (2020) Enzymes DOI: 10.1016/bs.enz.2020.05.011
  • A. Kumpf, D. Kowalczykiewicz, K. Szymańska, M. Mehnert, I. Bento, A. Łochowicz, A. Pollender, A. Jarzȩbski, D. Tischler, Immobilization of the highly active UDP-glucose pyrophosphorylase from Thermocrispum agreste provides a highly efficient biocatalyst for the production of UDP-glucose (2020) Front. Bioeng. Biotechnol. DOI: 10.3389/fbioe.2020.00740
  • D. Eggerichs, C. Mügge, J. Mayweg, U.-P. Apfel, D. Tischler, Enantioselective epoxidation by flavoprotein monooxygenases supported by organic solvents (2020) Catalysts DOI: 10.3390/catal10050568
  • M. Hofmann, G. Retamal-Morales, D. Tischler, Metal binding ability of microbial natural metal chelators and potential applications (2020) Nat. Prod. Rep. DOI: 10.1039/C9NP00058E
  • A. Maier, S. Wansel, A.G. Baraibar, C. Mügge, D. Tischler, N-hydroxydiamines - Versatile components for the synthesis of active ingredients (2020) BioSpektrum DOI: 10.1007/s12268-020-1374-6
  • R. Schwabe, C.H.R. Senges, J.E. Bandow, T. Heine, H. Lehmann, O. Wiche, M. Schlömann, G. Levicán, D. Tischler, Cultivation dependent formation of siderophores by Gordonia rubripertincta CWB2 (2020) Microbiol. Res. DOI: 10.1016/j.micres.2020.126481
  • R. Schwabe, C.H.R. Senges, J.E. Bandow, T. Heine, H. Lehmann, O. Wiche, M. Schlömann, G. Levicán, D. Tischler, Data on metal-chelating, -immobilisation and biosorption properties by Gordonia rubripertincta CWB2 in dependency on rare earth adaptation (2020) Data in Brief DOI: 10.1016/j.dib.2020.105739
  • M. Hofmann, J.S. Martin del Campo, P. Sobrado, D. Tischler, Biosynthesis of desferrioxamine siderophores initiated by decarboxylases: A functional investigation of two lysine/ornithine-decarboxylases from Gordonia rubripertincta CWB2 and Pimelobacter simplex 3E (2020) Arch. Biochem. Biophys. DOI: 10.1016/
  • M.J.C. Espinosa, A.C. Blanco, T. Schmidgall, A.K. Atanasoff-Kardjalieff, U. Kappelmeyer, D. Tischler, D.H. Pieper, H.J. Heipieper, C. Eberlein, Toward biorecycling: isolation of a soil bacterium that grows on a polyurethane oligomer and monomer (2020) Front. Microbiol. DOI 10.3389/fmicb.2020.00404
  • S. Kumaran, A.C.R. Ngo, F.P.J. Schultes, D. Tischler, Draft genome sequence of Kocuria indica DP-K7, a methyl red degrading actinobacterium (2020) 3 Biotech DOI: 10.1007/s13205-020-2136-3
  • D. Tischler, E. Gädke, D. Eggerichs, A. Gomez Baraibar, C. Mügge, A. Scholtissek, C.E. Paul, Asymmetric reduction of (R)-carvone through a thermostable and organic-solvent-tolerant ene-reductase (2020) ChemBioChem DOI: 10.1002/cbic.201900599
  • C. Willrodt, J.A.D. Gröning, P. Nerke, R. Koch, A. Scholtissek, T. Heine, A. Schmid, B. Bühler, D. Tischler, Highly efficient access to (S)-sulfoxides utilizing a promiscuous flavoprotein monooxygenase in a whole-cell biocatalyst format (2020) ChemCatChem DOI: 10.1002/cctc.201901894
  • M. Hofmann, T. Heine, V. Schulz, S. Hofmann, D. Tischler, Draft genomes and initial characterization of siderophore producing pseudomonads isolated from mine dump and mine drainage (2020) Biotechnol. Rep. DOI: 10.1016/j.btre.2019.e00403
  • T. Heine, A. Scholtissek, S. Hofmann, R. Koch, D. Tischler, Accessing enantiopure epoxides and sulfoxides: Related flavin-dependent monooxygenases provide reversed enantioselectivity (2020) ChemCatChem DOI: 10.1002/cctc.201901353
  • A.C. Lienkamp, T. Heine, D. Tischler, Glutathione: A powerful but rare cofactor among Actinobacteria (2020) Adv. Appl. Microbiol. DOI: 10.1016/bs.aambs.2019.12.003
  • L. Mestrom, M. Przypis, D. Kowalczykiewicz, A. Pollender, A. Kumpf, I. Bento, A. Jarzebski, K. Szymańska, A. Chruściel, D. Tischler, R. Schoevaart, P.-L. Hagedoorn, U. Hanefeld, Leloir glycosyltransferases in applied biocatalysis: A multidisciplinary approach (2019) Int. J. Mol. Sci. DOI: 10.3390/ijms20215263
  • A. Kumpf, A. Partzsch, A. Pollender, I. Bento, D. Tischler, Two homologous enzymes of the GalU family in Rhodococcus opacus 1CP – RoGalU1 and RoGalU2 (2019) Int. J. Mol. Sci. DOI: 10.3390/ijms20225809
  • D. Eggerichs, A.C. Lienkamp, T. Heine, C. Mügge, D. Tischler, Chiral epoxidation of aryl-alkyl ethers from lignin (Chirale Epoxidierung von Aryl-Alkyl-Ethern aus Lignin) (2019) BIOspektrum DOI: 10.1007/s12268-019-0219-7
  • R. Schwabe, B. Obst, M. Mehnert, D. Tischler, O. Wiche, Influence of pH and presence of bacterial siderophores on the mobilization of trace elements in soil extracts (Mobilisierung von Spurenelementen in Bodenextrakten durch bakterielle Siderophore in Abhängigkeit des pH-Wertes) (2019) F. Ecol. Online
  • D.N. Proença, T. Heine, C.H. Senges, J.E. Bandow, P.V. Morais, D. Tischler, Bacterial metabolites produced under iron limitation kill pinewood nematode and attract Caenorhabditis elegans (2019) Front. Microbiol. DOI: 10.3389/fmicb.2019.02166
  • D. Tischler, W.J.H van Berkel, M.W. Fraaije, Actinobacteria, a source of biocatalytic tools (2019) Front. Microbiol.: DOI: 10.3389/fmicb.2019.00800
  • T. Heine, C. Großmann, S. Hofmann, D. Tischler, Indigoid dyes by group E monooxygenases: mechanism and biocatalysis (2019) Biol. Chem.: DOI: 10.1515/hsz-2019-0109
  • J. Enoki, M. Linhorst, F. Busch, A. Gomez-Baraibar, K. Miyamoto, R. Kourist, C. Mügge, Preparation of optically pure flurbiprofen via an integrated chemo-enzymatic synthesis pathway (2019) Mol. Catal.: DOI: 10.1016/j.mcat.2019.01.024
  • J. Enoki, C. Mügge, D. Tischler, K. Miyamoto, R. Kourist, Chemoenzymatic cascade synthesis of optically pure alkanoic acids using engineered arylmalonate decarboxylase variants (2019) Chem. Eur. J.: DOI: 10.1002/chem.201806339
  • A.H. Westphal, D. Tischler, F. Heinke, S. Hofmann, J.A.D. Gröning, D. Labudde, W.J.H. van Berkel, Pyridine Nucleotide Coenzyme Specificity of p-Hydroxybenzoate Hydroxylase and Related Flavoprotein Monooxygenases (2018) Front. Microbiol.: DOI: 10.3389/fmicb.2018.03050
  • R. Schwabe, M.K. Anke, K. Szymańska, O. Wiche, D. Tischler, Analysis of desferrioxamine-like siderophores and their capability to selectively bind metals and metalloids: development of a robust analytical RP-HPLC method (2018) Res. Microbiol.: DOI: 10.1016/j.resmic.2018.08.002.
  • A. Scholtissek, E. Gädke, C.E. Paul, A.H. Westphal, W.J.H. van Berkel, D. Tischler, Catalytic performance of a class III Old yellow enzyme and its cysteine variants (2018) Front. Microbiol.: DOI: 10.3389/fmicb.2018.02410.
  • J. Trögl, C.O. Esuola, S. Kříženecká, P. Kuráň, L. Seidlová, P. Veronesi-Dáňová, J. Popelka, O.O. Babalola, P. Hrabák, M. Czinnerová, E. Kakosová, A. Ševců, D. Tischler, Biodegradation of high concentrations of aliphatic hydrocarbons in soil from a petroleum refinery: Implications for applicability of new actinobacterial strains (2018) Appl. Sci.: DOI: 10.3390/app8101855.
  • T. Heine, W.J.H. van Berkel, G.T. Gassner, K.H. van Pée, D. Tischler, Two-component fad-dependent monooxygenases: Current knowledge and biotechnological opportunities (2018) Biology: DOI: 10.3390/biology7030042.
  • G. Retamal-Morales, T. Heine, J.S. Tischler, B. Erler, J.A.D. Gröning, S.R. Kaschabek, M. Schlömann, G. Levicán, D. Tischler, Draft genome sequence of Rhodococcus erythropolis B7g, a biosurfactant producing actinobacterium (2018) J. Biotechnol.: DOI: 10.1016/j.jbiotec.2018.06.001.
  • T. Heine, C. Großmann, S. Hofmann, D. Tischler, Enzymgesteuerte Indigoproduktion (2018) BioSpektrum: DOI: 10.1007/s12268-018-0938-1
  • T. Heine, J. Zimmerling, A. Ballmann, S.B. Kleeberg, C. Rückert, T. Busche, A. Winkler, J. Kalinowski, A. Poetsch, A. Scholtissek, M. Oelschlägel, G. Schmidt, D. Tischler, On the enigma of glutathione-dependent styrene degradation in Gordonia rubripertincta CWB2 (2018) Appl. Environ. Microbiol.: DOI: 10.1128/AEM.00154-18.
  • G. Retamal-Morales, M. Mehnert, R. Schwabe, D. Tischler, M. Schlömann, G. Levicán, Detection of arsenic-binding siderophores in arsenic-tolerating Actinobacteria by a modified CAS assay (2018) Ecotoxicol. Environ. Saf.: DOI: 10.1016/j.ecoenv.2018.03.087
  • M. Oelschlägel, J. Zimmerling, D. Tischler, A review: The styrene metabolizing cascade of side-chain oxygenation as biotechnological basis to gain various valuable compounds (2018) Front. Microbiol.: DOI: 10.3389/fmicb.2018.00490
  • D. Tischler, R. Schwabe, L. Siegel, A. Scholtissek, T. Heine, VpStyA1/VpStyA2B of variovorax paradoxus EPS: An aryl alkyl sulfoxidase rather than a styrene epoxidizing monooxygenase (2018) Molecules: DOI: 10.3390/molecules23040809
Publications of the Junior Research Group ChemBioCat headed by Professor Kourist
  • S. Bojarra, D. Reichert, M. Grote, A. Gómez-Baraibar, A. Dennig, B. Nidetzky, C. Mügge, R. Kourist, Bio‐based α,ω‐Functionalized Hydrocarbons from Multi‐step Reaction Sequences with Bio‐ and Metallo‐catalysts Based on the Fatty Acid Decarboxylase OleTJE (2017) ChemCatChem: DOI: 10.1002/cctc.201701804
  • S. Böhmer, K. Köninger, A. Gómez-Baraibar, S. Bojarra, C. Mügge, S. Schmidt, M. Nowaczyk, R. Kourist, Enzymatic Oxyfunctionalization Driven by Photosynthetic Water-Splitting in the Cyanobacterium Synechocystis sp. PCC 6803 (2017) Catalysts: DOI: 10.3390/catal7080240
  • M. Aßmann, C. Mügge, S. Gaßmeyer, J. Enoki, L. Hilterhaus, R. Kourist, A. Liese, S. Kara, Improvement of the Process Stability of Arylmalonate Decarboyxlase by Immobilization for Biocatalytic Profen Synthesis (2017) Front. Microbiol.: DOI: 10.3389/fmicb.2017.00448
  • A. Gómez-Baraibar, D. Reichert, C. Mügge, S. Seger, H. Gröger and R. Kourist, A sequential one-pot cascade reaction combining an encapsulated decarboxylase with metathesis for the synthesis of bio-based antioxidants (2016) Ang. Chem., Int. Ed.: DOI: 10.1002/anie.201607777
  • J. Enoki, J. Meisborn, A. Müller and R. Kourist, A multi-enzymatic cascade reaction for the stereoselective production of γ-oxyfunctionalyzed amino acids (2016) Front. Microbiol.: DOI: 10.3389/fmicb.2016.00425.
  • K. Köninger, A. Gómez-Baraibar, C. Mügge, C. Paul., F. Hollmann, M. Nowaczyk and R. Kourist, Recombinant cyanobacteria as tools for asymmetric C=C bond reduction fueled by biocatalytic water oxidation (2016) Ang. Chem., Int. Ed.: DOI: 10.1002/anie.201601200/full
  • F. Busch, N. Hülsemann, J. Enoki, K. Miyamoto, M. Bocola and R. Kourist, Semiempirical QM/MM calculations reveal a step-wise proton transfer and an unusual thiolate pocket in the mechanism of the racemizing mutant G74C of arylmalonate decarboxylase (2016) Catalysis Science & Technology: DOI: 10.1039/C5CY01964H
  • S. K. Gaßmeyer, J. Wetzig, C. Mügge, M. Assmann, J. Enoki, L. Hilterhaus, R. Zuhse, K. Miyamoto, A. Liese and R. Kourist, Arylmalonate decarboxylase-catalyzed asymmetric synthesis of both enantiomers of optically pure flurbiprofen (2015) ChemCatChem: DOI: 10.1002/cctc.201501205.
  • S. K. Gaßmeyer, H. Yoshikawa, J. Enoki, N. Hülsemann, R. Stoll, K. Miyamoto and R. Kourist, STD-NMR based protein engineering of the unique arylpropionate-racemase AMDase G74C (2015), ChemBioChem, 16, 1943-1949.
  • S. Yoshida, J. Enoki, R. Kourist, K. Miyamoto, Engineered hydrophobic pocket of (S)-selective arylmalonate decarboxylase variant by simultaneous saturation mutagenesis to improve catalytic performance (2015) Bioscience, Biotechnology and Biochemistry, doi: 10.1080/09168451.2015.1060844.
  • S. Yoshida, J. Enoki, R. Hemmi, R. Kourist, N. Kawakami, and K. Miyamoto, Draft genome sequence of Bordetella bronchiseptica KU1201, the first isolation source of arylmalonate decarboxylase (2015) Genome Announcements, 3, e00373-15.