Lanza, L., Rabe von Pappenheim, F., Bjarnesen, D., Leogrande, C., Paul, A., Krug, L., Tittmann, K. & Müller, M. (2024) Identification and Characterization of Thiamine Diphosphate-Dependent Lyases with an Unusual CDG Motif. Angewandte Chemie 2024, accepted.

Tamhankar, A., Wensien, M., Jannuzzi, S. A. V., Chatterjee, S., Lasalle-Kaiser, B., Tittmann, K.* & DeBeer, S.* (2024) In solution identification of the lysine-cysteine redox switch with a NOS bridge in Transaldolase by Sulfur K-edge X-ray Absorption Spectroscopy. Journal of Physical Chemistry Letters 15(16), 4263-4267.

Funk, L.-M., Poschmann, G., Rabe von Pappenheim, F., Chari, A., Stegmann, K. M., Dickmanns, A., Wensien, M., Eulig, N., Paknia, E., Heyne, G., Penka, E., Pearson, A. R., Berndt, C., Fritz, T., Bazzi, S., Uranga, J., Mata, R. A., Dobbelstein, M., Hilgenfeld, R., Curth, U. & Tittmann, K. (2024) Multiple redox switches of the SARS-CoV-2 main protease in vitro provide opportunities for drug design. Nature Communications 15, 411.


Liu, Z., Xiao, C., Lin, S., Tittmann, K. * & Dai, S. * (2023) Multifaceted role of the substrate phosphate group in transketolase catalysis. ACS Catalysis 14, 355–365.

Uranga, J., Rabe von Pappenheim, F., Tittmann, K. & Mata, R. A. (2023) Dynamic Protonation States Underlie Carbene Formation in ThDP-Dependent Enzymes: A Theoretical Study. Journal of Physical Chemistry B 127, 9423−9432.

Ye, J., Bazzi, S., Fritz, T., Tittmann, K., Mata, R. A. & Uranga, J. (2023) Mechanisms of Cysteine‐Lysine Covalent Linkage ‐ The Role of Reactive Oxygen Species and Competition with Disulfide Bonds. Angewandte Chemie 2023, e202304163.

Hicks, K. G., Cluntun, A. A., ..., Prajapati, S., ..., Tittmann, K., ..., Rutter, J. (2023) Protein-metabolite interactomics of carbohydrate metabolism reveal regulation of lactate dehydrogenase. Science 379, 996–1003.


Prajapati, S., Rabe von Pappenheim, F., Tittmann, K. (2022) Frontiers in the enzymology of thiamin diphosphate-dependent enzymes. Current Opinion in Structural Biology 76,102441.

Meyer, A., Kehl, A., Cui, C., Reichardt, F.A.K., Hecker, F., Funk, L.-M., Pan, K.-T., Urlaub, H., Tittmann, K., Stubbe, J., Bennati, M. (2022) 19F Electron Nuclear Double Resonance reveals interaction between redox active tyrosines across the alpha/beta interface of E. coli ribonucleotide reductase. J. Am. Chem. Soc. 144 (25), 11270–11282.

Rindfleisch, S., Krull, M., Uranga, J., Schmidt, T., Rabe von Pappenheim, F., Kirck, L. L., Balouri, A., Schneider, T., Chari, A., Kluger, R., Bourenkov, G., Diederichsen, U., Mata, R. A. Tittmann, K. (2022) Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5′-monophosphate decarboxylase catalysis. Nature Catalysis 5, 332–341.

Rabe von Pappenheim, F. & Tittmann, K. (2022) Lysines and cysteines: Partners in stress? Trends in Biochemical Sciences 47(5), 372-374.

Rabe von Pappenheim, F., Wensien, M., Ye, J., Uranga, J., Irisarri, I., de Vries, J., Funk, L.-M., Mata, R. & Tittmann, K. (2022) Widespread occurrence of covalent lysine–cysteine redox switches in proteins. Nature Chemical Biology 18, 368–375 .


Nair, A., Goyal, I., Voß, E., Mrozek, P., Prajapati, S., Thurow, C., Tietze, L., Tittmann, K. and Gatz, C. (2021) NPR1 and TGA factors are required for N-hydroxypipecolic acid-induced signaling at basal salicylic acid levels. Plant Physiology 187 (4), 2803–2819.

Wensien, M., Rabe von Pappenheim, F., Funk, L.-M., Kloskowski, P., Curth, U., Diederichsen, U., Uranga, J., Ye, J., Fang, P., Pan, K.-T, Urlaub, H., Mata, R. A., Sautner, V. & Tittmann, K. (2021). A lysine–cysteine redox switch with an NOS bridge regulates enzyme function. Nature 593, 460-464.

Perera, R.P., Shaikhqasem, A., Rostam, N., Dickmanns, A., Ficner, R., Tittmann, K., Dosch, R. (2021) Bucky Ball Is a Novel Zebrafish Vasa ATPase Activator. Biomolecules 11, 1507


Rabe von Pappenheim, F., Aldeghi, M., Shome, B., Begley, T., de Groot, B. L. & Tittmann, K. (2020) Structural basis for antibiotic action of the B1 antivitamin 2’-methoxy-thiamine. Nature Chemical Biology 16(11),1237-1245.

Kupski, O., Funk, L.-M., Sautner, V., Seifert, F., Worbs, B., Ramsbeck, D., Meyer, F., Diederichsen, U., Buchholz, M., Schilling, S., Demuth, H.-U., Tittmann, K. (2020) Hydrazides are potent transition-state analogs for glutaminyl cyclase implicated in the pathogenesis of Alzheimer’s Disease. Biochemistry, 59, 2585–2591.

Roth, S., Stockinger, P., Steff, J., Steimle, S., Sautner, V., Tittmann, K., Pleiss, J. & Müller, M. (2020) Crossing the Border: From Keto- to Imine Reduction in Short-Chain Dehydrogenases/Reductases. ChemBioChem 21, 2615 – 2619.

Singh, K., Graf, B., Linden, A., Sautner, V., Urlaub, H., Tittmann, K., Stark, H. & Chari, A. (2020) Discovery of a regulatory subunit of the yeast fatty acid synthase. Cell 180, 1130-1143.


Dai, S., Funk, L.-M., Rabe von Pappenheim, F., Sautner, V., Paulikat, M., Schröder, B., Uranga, J., Mata, R. A. & Tittmann, K. (2019) Low-barrier hydrogen bonds in enzyme cooperativity. Nature 573, 609–613.

Prajapati, S., Haselbach, D., Wittig, S., Patel, M. S., Chari, A., Schmidt, C., Stark, H. & Tittmann, K. (2019) Structural and functional analysis of the human pyruvate dehydrogenase complex suggest a “division-of-labor” mechanism by local E1 and E3 clusters. Structure 27, 1124-1136.


Paulikat, M., Wechsler, C., Tittmann, K. & Mata, R. A. (2017) Theoretical Studies of the Electronic Absorption Spectra of Thiamin Diphosphate in Pyruvate Decarboxylase. Biochemistry 56, 1854-1864.


Schrader, J., Henneberg, F., Mata, R., Tittmann, K., Schneider, T. R., Stark, H., Bourenkov, G. & Chari, A. (2016) The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design. Science 353, 594-598.

Andrews, F. H., Wechsler, C., Rogers, M. P., Meyer, D., Tittmann, K. & McLeish, M.J. (2016) Mechanistic and Structural Insight to an Evolved Benzoylformate Decarboxylase with Enhanced Pyruvate Decarboxylase Activity. Catalysts 6, 190.

Pérez-Lara, A., Thapa, A., Nyenhuis, S. B., Nyenhuis, D. A., Halder, P. ,Tietzel, M., Tittmann, K., Cafiso, D. S. & Jahn, R. (2016) PtdInsP2 and PtdSer cooperate to trap synaptotagmin-1 to the plasma membrane in the presence of calcium. eLife, 5:e15886 (

Affaticati, P., Dai, S., Payongsri, P., Hailes, H., Tittmann, K.* & Dalby, P.* (2016) Structural Analysis of an Evolved Transketolase Reveals Divergent Binding Modes. Scientific Reports 6, 35716.


Wechsler, C., Meyer, D., Loschonsky, S., Funk, L.-M., Neumann, P., Ficner, R., Brodhun, F., Müller, M. & Tittmann, K. (2015) Tuning and switching enantioselectivity of asymmetric carboligation in an enzyme through mutational analysis of a single hot spot. ChemBioChem 16(18), 2580-4.

Chari, A., Haselbach, D., Kirves, J.-M., Ohmer, J., Paknia, E., Fischer, N., Ganichkin, O., Möller, V., Frye, J. J., Petzold, G., Jarvis, M., Tietzel, M., Grimm, C., Peters, J.-M., Schulman, B., Tittmann, K., Markl, J., Fischer, U. & Stark, H. (2015) ProteoPlex - stability optimization of macromolecular complexes by sparse-matrix screening of chemical space. Nature Methods 12, 859-865.

Sautner, V., Friedrich, M.-M., Lehwess-Litzmann, A. & Tittmann, K. (2015) Converting transaldolase into aldolase through swapping of the multifunctional acid-base catalyst. COMMON AND DIVERGENT CATALYTIC PRINCIPLES IN F6P ALDOLASE AND TRANSALDOLASE. Biochemistry 54, 4475-4486.

Seifert, F., Demuth, H.-U., Weichler, T., Ludwig, H. H., Tittmann, K. & Schilling, S. (2015) Phosphate Ions and Glutaminyl Cyclases Catalyse the Cyclization of Glutaminyl Residues by Facilitating Synchronized Proton Transfers. Bioorg. Chem. 60, 98-101.

Brodhun, F. & Tittmann, K. (2015) Membrane enzymes: Transformers at the interface. Nature Chem. Biol. 11, 102-103.


Gundlach, J., Dickmanns, A., Schröder-Tittmann, K., Neumann, P., Kampf, J., Herzberg, C., Hammer, E., Schwede, F., Kaever, V., Tittmann, K., Stülke, J. & Ficner, R. (2014) Identification, characterization and structure analysis of the c-di-AMP binding PII-like signal transduction protein DarA. J. Biol. Chem. , 290(5):3069-80.

Neumann, P. & Tittmann, K. (2014) Marvels of enzyme catalysis at true atomic resolution: Distortions, bond elongations, hidden flips, protonation states and atom identities. Curr. Opin. Struct. Biol. 29, 122-133.

Tittmann, K. (2014) Sweet siblings with different faces: the mechanisms of FBP and F6P aldolase, transaldolase, transketolase and phosphoketolase revisited in light of recent structural data. Bioorg. Chem. 57, 263-280.

Mehne, F. M. P., Schröder-Tittmann, K., Eijlander, R., Herzberg, C., Hewitt, L., Kaever, V., Leweis, R. J., Kuipers, O. P., Tittmann, K., Stülke, J. (2014) Control of the Diadenylate Cyclase CdaS in Bacillus subtilis: An Autoinhibitory Domain Limits c-di-AMP Production. J. Biol. Chem. 289(30), 21098-107.


Lüdtke, S., Neumann, P., Erixon, K. M., Leeper, F., Kluger, R., Ficner, R., Tittmann, K. (2013) Sub-Angström resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate. Nature Chem. 5, 762-767.

Meyer, D., Neumann, P., Ficner, R., Tittmann, K. (2013) Observation of a stable carbene at the active site of a thiamin enzyme. Nature Chem. Biol. 9, 488-490.

Schröder-Tittmann, K., Meyer, D., Arens, J., Wechsler, C., Tietzel, M., Golbik, R., Tittmann, K. (2013) Alternating Sites Reactivity Is a Common Feature of Thiamin Diphosphate-Dependent Enzymes As Evidenced by Isothermal Titration Calorimetry Studies of Substrate Binding. Biochemistry 52(15):2505-2507.


Schneider, S., Lüdtke, S., Schröder-Tittmann, K., Wechsler, C., Meyer, D., Tittmann, K. (2012) A DELTA 38 deletion variant of human transketolase as a model of transketolase-like protein 1 exhibits no enzymatic activity. PLoS ONE 7(10): e48321.

Meyer, D., Neumann, P., Koers, E., Sjuts, H., Lüdtke, S., Sheldrick, G. M., Ficner, R., Tittmann, K. (2012) Unexpected tautomeric equilibria of the carbanion-enamine intermediate in pyruvate oxidase highlight unrecognized chemical versatility of the thiamin cofactor. Proc. Natl. Acad. Sci. USA. 109(27):10867-72.

Belenky, I., Steinmetz, A., Vyazmensky, M., Barak, Z., Tittmann, K., Chipman, D. M. (2012) Many of the functional differences between Acetohydroxyacid Synthase isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-ThDP adduct in AHAS I. FEBS J. 279(11):1967-79.

Balakrishnan, A., Gao, Y., Moorjani, P., Nemeria, N., Tittmann, K., Jordan, F. (2012) Bifunctionality of the thiamin diphosphate cofactor: Assignment of tautomeric/ionization states of the 4'-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylase. J. Am. Chem. Soc. 134(8):3873-85.


Lehwess-Litzmann, A., Neumann, P., Parthier, C., Lüdtke, S., Golbik, R., Ficner R., Tittmann, K. (2011) Twisted Schiff-base Intermediates and Substrate Locale Revise Transaldolase Mechanism. Nature Chem. Biol. 7, 678-684.

Lehwess-Litzmann, A., Neumann, P., Golbik, R., Parthier, C., Tittmann, K. (2011) Crystallization and preliminary X-ray diffraction analysis of transaldolase from Thermoplasma acidophilum. Acta Cryst Sect F 67, 584-586.

Vyazmensky, M., Steinmetz, A., Meyer, D., Golbik, R. , Barak, Z., Tittmann, K.* & Chipman, D. M.* (2011) Polar residues playing significant roles in catalysis by acetohydroxyacid 2 synthase isozyme II from Escherichia coli: Glu47, Gln110, Lys159 and His251. Biochemistry 50, 3250-3260.

Meyer, D., Walter, L., Kolter, G. Pohl, M., Müller, M. & Tittmann, K. (2011) Conversion of pyruvate decarboxylase into an enantioselective carboligase with biosynthetic potential. J. Am. Chem. Soc. 133, 3609-3616.

Helfmann, S., Neumann, P., Tittmann, K., Moser, T., Ficner, R., Reisinger, E. (2010) The crystal structure of the C2A domain of otoferlin reveals an unconventional top loop region. J. Mol. Biol. 406, 479-490.

Nadler, A., Koch, C., Brodhun, F., Wehland, J.-D., Tittmann, K., Feussner, I. & Diederichsen, U. (2011) Influence of substrate dideuteration on the reaction of the bifunctional heme enzyme psi factor producing oxygenase A (PpoA). ChemBioChem 12, 728-737.


Mitschke, L., Parthier, C., Schröder-Tittmann, K., Coy, J., Lüdtke, S. & Tittmann, K. (2010) The crystal structure of human transketolase and new insights into its mode of action. J. Biol. Chem. 285, 31559-31570.

Meyer, D., Neumann, P., Parthier, C., Friedemann, R., Nemeria, N., Jordan, F. & Tittmann, K. (2010) Double duty for a conserved glutamate in pyruvate decarboxylase: evidence of the participation in stereoelectronically controlled decarboxylation and in protonation of the nascent carbanion/enamine intermediate. Biochemistry 49, 8197-8212.

Schröder-Tittmann, K., Bosse-Doenecke, E., Reedtz-Runge, S., Ihling, C., Sinz, A., Tittmann, K. & Rudolph R. (2010) Recombinant expression, in vitro refolding, and biophysical characterization of the human glucagon-like peptide-1 receptor. Biochemistry 49, 7956-7965.

Steinmetz, A., Vyazmensky, M., Meyer, D., Barak, Z. E., Golbik, R., Chipman, D. M. & Tittmann, K. (2010) Valine 375 and phenylalanine 109 confer affinity and specificity for pyruvate as donor substrate in acetohydroxy acid synthase isozyme II from Escherichia coli. Biochemistry 49, 5188-5199.

Nemeria, N.S., Arjunan, P., Chandrasekhar, K., Mossad, M., Tittmann, K., Furey, W. & Jordan, F. (2010) Communication between thiamin cofactors in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers: evidence for a "direct pathway" between the 4'-aminopyrimidine N1' atoms. J. Biol. Chem. 285, 11197-11209.


Tittmann, K. & Wille, G. (2009) X-ray crystallographic snapshots of reaction intermediates in pyruvate oxidase and transketolase illustrate common themes in thiamin catalysis. J. Mol. Cat. B: Enzymatic 61, 93-99.

Weidner, A., Neumann, P., Pech, A., Stubbs, M. T. & Tittmann, K. (2009) New insights into the membrane-binding and activation mechanism of pyruvate oxidase from Escherichia coli. J. Mol. Cat. B: Enzymatic 61, 88-92.

Chipman, D., Barak, Z., Shaanan, B., Vyazmensky, M., Binshtein, E., Belenky, I., Temam, V., Steinmetz, A., Golbik, R. & Tittmann, K. (2009) Origin of the Specificities of Acetohydroxy-acid Synthases and Glyoxylate Carboligase. J. Mol. Cat. B: Enzymatic 61, 50-55.

Fraas, S., Steinbach, A., Tabbert, A., Harder, J., Ermler, U., Tittmann, K., Meyer, A. & Kroneck, P. (2009) Cyclohexane-1,2-dione Hydrolase: a new tool to degrade alicyclic compounds. J. Mol. Cat. B: Enzymatic 61, 47-49.

Kokova, M., Zavrel, M., Tittmann, K., Spiess, A. & Pohl, M. (2009) Investigating the Carboligase Activity of Thiamine Diphosphate-dependent Enzymes Using Kinetic Modeling and NMR Spectroscopy. J. Mol. Cat. B: Enzymatic 61, 73-79.

Friedemann, R., Tittmann, K., Golbik, R. & Hübner, G. (2009) DFT and MP2 Studies on the C2-C2alpha Bond Cleavage in Thiamin Catalysis. J. Mol. Cat. B: Enzymatic 61, 36-38.

Meshalkina, L., Kochetov, G., Hübner, G., Tittmann, K. & Golbik, R. (2009) Steric and electronic properties of the cofactor�s amino group control the lifetime of the central carbanion/enamine intermediate in transketolase. J. Mol. Cat. B: Enzymatic 61, 67-72.

Tittmann, K. (2009) Thiamin diphosphate in biological chemistry: applications in biocatalysis, coenzyme analogues as mechanistic probes and natural derivatives of thiamin. FEBS J. 276, 2893. Editorial.

Tittmann, K. (2009) Reaction mechanisms of thiamin diphosphate enzymes: redox reactions. FEBS J. 276, 2454-68.

Tittmann, K. (2009) Reaction mechanisms of thiamin diphosphate enzymes. FEBS J. 276, 2431. Editorial.

Meshalkina, L., Kochetov, G., Hübner, G., Tittmann, K. & Golbik, R. (2009) New function of the amino group of thiamine diphosphate in thiamine catalysis. Biochemistry (Mosc.) 74, 293-300.

Bruning, M., Berheide, M., Meyer, D., Golbik, R., Bartunik, H., Liese, A. & Tittmann, K. (2009) Structural and kinetic studies on native intermediates and an intermediate analogue in benzoylformate decarboxylase reveal a least-motion mechanism with an unprecedented short-lived pre-decarboxylation intermediate. Biochemistry 48, 3258-3268.

Liavonchanka, A., Rudolph, M., Tittmann, K., Hamberg, M. & Feussner, I. (2009) On the mechanism of a polyunsaturated fatty acid double bond isomerase from Propioni-bacterium acnes. J. Biol. Chem. 284, 8005-8012.


Neumann, P., Weidner, A., Pech, A., Stubbs, M. T. & Tittmann, K. (2008) Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from E. coli. Proc. Natl. Acad. Sci. USA 105, 17390-5.

Kluger, R. & Tittmann, K. (2008) Thiamin Diphosphate Catalysis: Enzymic and Nonenzymic Covalent Intermediates. Chem. Rev. 108, 1797-1833.

Weidner, A., Neumann, P., Wille, G., Stubbs, M. T. & Tittmann, K. (2008) Crystallization and preliminary X-ray diffraction analysis of full-length and proteolytically activated pyruvate oxidase from Escherichia coli. Acta Cryst Sect F 64 (3), 179-181.

Kaplun, A., Binshtein, E., Vyazmensky, M., Steinmetz, A., Barak, Z., Chipman, D., Tittmann, K. & Shaanan, B. (2008) Glyoxylate carboligase lacks the canonical active site glutamate of thiamin-dependent enzymes. Nature Chem. Biol. 4 (2), 113-118.

Werther, T., Spinka, M. Tittmann, K., Schütz, A., Golbik, R., Mrestani-Claus, C., Hübner, G. & König, S. (2008) Amino acids allosterically regulate the thiamine diphosphate-dependent -keto acid decarboxylase from mycobacterium tuberculosis. J. Biol. Chem. 283, 5344-5354.

Meshalkina, L., Kochetov, G., Brauer, J., Hübner, G. Tittmann, K. & Golbik, R. (2008) New evidence for cofactor amino group function in thiamine catalysis on the example of transketolase. Biochem. Biophys. Res. Comm. 366, 692-697.

2007 -1997

Seifert, F., Ciszak, E., Korotchkina, L.G., Golbik, R., Spinka, M., Dominiak, P., Sidhu, S., Brauer, J., Patel., M.S. & Tittmann, K. (2007) Phosphorylation of serine 264 impedes active site accessibility in E1 component of human pyruvate dehydrogenase multienzyme complex. Biochemistry 46, 6277-6287.

Asztalos, P., Parthier, C., Golbik, R., Kleinschmidt, M., Hübner, G., Weiss, M. S., Wille, G. & Tittmann, K. (2007) Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry 46, 12037-12052.

Joseph, E., Wei, W., Tittmann, K. & Jordan, F. (2006) Function of a conserved loop of the beta-domain, not involved in thiamin diphosphate binding, in catalysis and substrate activation in yeast pyruvate decarboxylase. Biochemistry 45, 13517-13527.

Seifert, F., Golbik, R., Brauer, J., Lilie, H., Schröder-Tittmann, K., Hinze, E., Korotchkina, L.G., Patel, M.S. & Tittmann, K. (2006) Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation. Biochemistry 45, 12775-12785.

Wille, G., Meyer, D., Steinmetz, A., Hinze, E., Golbik, R. & Tittmann, K. (2006) The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nature Chem. Biol. 2, 324-328.

Hübner, G., Golbik, R. & Tittmann, K. (2006) Hydrogen transfer in the action of thiamin diphosphate enzymes. In Handbook of hydrogen transfer in biological systems (Eds.: R. L. Schowen, J. Klinman).

Tittmann, K., Wille, G., Golbik, R., Weidner, A., Ghisla, S. & Hübner, G. (2005) A radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum. Kinetic coupling of intercofactor electron transfer with phosphate transfer via a transient FAD semiquinone/hydroxyethyl-ThDP radical pair. Biochemistry 44, 13291-13303.

Chipman, D. M., Duggleby, R. G. & Tittmann, K. (2005) Mechanism of Acetohydroxyacid Synthases. Curr. Opin. Chem. Biol. 9, 475-481.

Tittmann, K., Golbik, R., Neef, H., Hübner, G. & Kern, D. (2005) Kinetic control of thiamin diphosphate activation in enzymes studied by proton nitrogen correlated NMR spectroscopy. Biochemistry 44, 8697-8700.

Tittmann, K. (2005) Autopsie von Enzymvarianten. Aufklaerung molekularer Details der Enzymkatalyse. BIOforum 6/2005, 2-4.

Nemeria, N., Tittmann, K., Ebenzer, J., Zhou, L., Vazquez-Coll, M., Arjunan, P., Hübner, G., Furey, W. & Jordan, F. (2005) Glutamate 636 of the Escherichia coli pyruvate dehydrogenase multienzyme complex E1 component participates in active center communication and protects from carboligase side reaction with pyruvate. An engineered acetolactate synthase with unusual stereoselectivity. J. Biol. Chem. 280, 21473-21482.

Schütz, A., Golbik, R., König, S., Hübner, G. & Tittmann, K. (2005) Intermediates and transition states in thiamin diphosphate-dependent decarboxylases. A kinetic and NMR study on indolepyruvate decarboxylase using indolepyruvate, benzoylformate and pyruvate as substrates. Biochemistry 44, 6164-6179.

Vinogradov, M., Kaplun, A., Vyazmensky, M., Golbik, R., Tittmann, K., Uhlemann, K., Meshalkina, L., Barak, Z., Hübner, G., Chipman, D. (2005) Monitoring the acetohydroxyacid synthase reaction and related carboligations by circular dichroism spectroscopy. Anal. Biochem. 342, 126-133.

Golbik, R., Meshalkina, L., Sandalova, T., Tittmann, K., Fiedler, E., Neef, H., König, S., Kluger, R., Kochetov, G., Schneider, G. & Hübner, G. (2005) Effect of coenzyme modification on structural and catalytic properties of transketolase wildtype and the variant E418A from Saccharomyces cerevisiae. Contrasting protonation state requirements of ThDP in decarboxylases and transketolases. FEBS J. 272, 1326-1342.

Tittmann, K., Vyazmensky, M., Hübner, G., Barak, Z. & Chipman, D. (2005) The carboligation reaction of acetohydroxyacid synthase II: Steady state intermediate distribution in wild-type and mutants by NMR. Proc. Natl. Acad. Sci. USA 102, 553-558.

Tittmann, K., Schröder, K., Golbik, R., McCourt, J., Duggleby, R., Barak, Z., Hübner, G. (2004) Electron transfer in acetohydroxyacid synthase as a side reaction in catalysis. Implications for the reactivity and partitioning of the key intermediate alpha-hydroxyethyl-thiamin diphosphate in a nonredox flavoenzyme. Biochemistry 43, 8652-8661.

Friedemann, R., Tittmann, K., Golbik, R. & Hübner, G. (2004) Modelling of elementary steps in thiamin catalysis. Intl. J. Quant. Chem. 99, 109-114.

Tittmann, K., Golbik, R., Uhlemann, K., Khailova, L., Schneider, G., Patel, M., Jordan, F., Chipman, D.M., Duggleby, R.G. & Hübner, G. (2003). NMR analysis of covalent intermediates in thiamin diphosphate enzymes. Biochemistry (Accelerated Article) 42, 7885-7891.

Schütz, A., Golbik, R., Tittmann, K., Svergun, D.I., Koch, M.H.J., Hübner, G. & König, S. (2003) Studies on structure-function relationships of indolepyruvate decarboxylase from Enterobacter cloacae, a key enzyme of the indole acetic acid pathway. Eur. J. Biochem. 270, 2322-2331.

Tittmann, K., Golbik, R. & Hübner, G. (2003) Beobachtung von Enzymen bei der Arbeit. Untersuchung von Reaktionsmechanismen. Scientia halensis 03/2003, 27-30.

Tittmann, K., Golbik, R., Uhlemann, K., Khailova, L., Schneider, G., Patel, M., Jordan, F., Chipman, D.M., Duggleby, R.G. & Hübner, G. (2002) How thiamin is working in enzymes: Time-resolved NMR snapshots of ThDP-dependent enzymes in action. In: Thiamin: Catalytic Mechanisms and Role in Normal and Disease States, pp 57-76. (Dekker, New York).

Tittmann, K., Golbik, R., Ghisla, S. & Hübner, G. (2002) Phosphate mediates electron transfer in pyruvate oxidase. In: Flavins and Flavoproteins 2002 (Eds. N. Scrutton, R. Perham and S. Chapman).

Tittmann, K., Hübner, G., Barak, Z. & Chipman, D. (2002) Acetohydroxyacid synthase catalyses electron transfer between a-hydroxyethyl-thiamin diphosphate and FAD in a slow side reaction of catalysis. In: Flavins and Flavoproteins 2002 (Eds. N. Scrutton, R. Perham and S. Chapman).

Bar-Ilan, A., Balan, V., Tittmann, K., Golbik, R., Vyazmensky, M., Hübner, G., Barak, Z. & Chipman, D. (2001) Binding and Activation of Thiamin Diphosphate in Acetohydroxyacid Synthase. Biochemistry 40, 11946-11954.

Liu, M., Sergienko, EA., Guo, F., Wang, J., Tittmann, K., Hübner, G., Furey, W. & Jordan, F. (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions. Biochemistry 40, 7355-7368.

Wang, J., Golbik, R., Seliger, B., Spinka, M., Tittmann, K., Hübner, G. & Jordan, F. (2001) Consequences of a modified putative substrate-activation site on catalysis by yeast pyruvate decarboxylase. Biochemistry 40, 1755-1763.

Fiedler, E., Golbik, R., Schneider, G., Tittmann, K., Neef, H., König, S. & Hübner, G. (2001) Examination of donor substrate conversion in yeast transketolase. J. Biol. Chem. 276, 16051-16058.

Tittmann, K., Golbik, R., Ghisla, S. & Hübner, G. (2000) Mechanism of Elementary Catalytic Steps in Pyruvate Oxidase from Lactobacillus plantarum. Biochemistry 39, 10747-10754.

Tittmann, K., Golbik, R., Ghisla, S. & Hübner, G. (1999) Single Step Analysis of Pyruvate Oxidase from Lactobacillus plantarum. Kinetics, Mechanism and Regulation. In: Flavins and Flavoproteins 1999 (Eds. Ghisla, S.; Kroneck, P.; Macheroux, P.; Sund, H.) Agency for scientific publications, Berlin, 395-400.

Tittmann, K., Mesch, K., Pohl, M. & Hübner, G. (1998) Activation of Thiamine Diphosphate in Pyruvate Decarboxylase from Zymomonas mobilis. FEBS Lett. 441, 404-406.

Tittmann, K., Proske, D., Spinka, M., Ghisla, S., Rudolph, R., Hübner, G. & Kern, G. (1998) Activation of Thiamin Diphosphate and FAD in the Phosphate-Dependent Pyruvate Oxidase from Lactobacillus plantarum. J. Biol. Chem. 273, 12929-12934.

Hübner, G., Tittmann, K., Killenberg-Jabs, M., Schäffner, J., Spinka, M., Neef, H., Kern, D., Kern, G., Schneider, G., Wikner, C. & Ghisla, S. (1998) Activation of ThDP in Enzymes. Biochim. Biophys. Acta 1385, 221-228.

Kern, D., Kern, G., Neef, H., Tittmann, K., KillenbergG-Jabs, M., Wikner, C., Schneider, G. & Hübner, G. (1997) How Thiamine Diphosphate is Activated in Enzymes. Science 275, 67-70.