prof. Ing. Štefan Janeček, DrSc.

Oddelenie biológie

vysokoškolský učiteľ

Vedecko-pedagogická charakteristika – stiahni PDF

Tituly, hodnosti:

  • 1989 – Ing. Katedra biochemickej technológie, Chemicko-technologická fakulta STU v Bratislave
  • 1993 – CSc.
  • 2002 – DrSc.
  • 2015 – doc.
  • 2021 – prof.

Pracovisko:

  • 1993 – doteraz Ústav molekulárnej biológie SAV, Bratislava – vedúci vedecký pracovník, Laboratórium evolúcie proteínov – na Ústave molekulárnej biológie SAV v Bratislave https://imb.savba.sk/~janecek
  • 2001 – doteraz Odborný asistent, Katedra biológie, Univerzita sv. Cyrila a Metoda, Fakulta prírodných vied, Trnava, – hlavné vyučované predmety: Molekulovo-biologické databázy, Bioinformatika a Proteínový dizajn v bakalárskom a magisterskom stupni.

Hlavné oblasti vedeckého záujmu: ťažisko práce je teoretické in silico štúdium proteínov – ich štruktúr vo vzťahu k ich funkcii, vlastnostiam a evolúcii. Hlavný záujem je o enzýmy z alfa-amylázovej rodiny – v súčasnosti v rámci klasifikácie CAZy (Carbohydrate Active enZymes) ide o rodiny glykozidových hydroláz GH13 (tvorí klan GH-H s rodinami GH70 a GH77), GH57 a GH119 (prípadne GH31 a GH126). Rovnaká pozornosť je venovaná aj bioinformatickým prístupom k štúdiu škrob-viažucich domén amylolytických enzýmov a ich analógov v neamylolytických enzýmoch a proteínoch, klasifikovaných do tzv. rodín CBM (carbohydrate-binding module families).

Vedenie prác (obhájené):

Bakalárske ; Diplomové ; Rigorózne ; Doktorandské

Členstvo v skúšobných komisiách, vo vedeckých radách, v odborných, habilitačných a inauguračných komisiách:

  • člen komisie pre štátne skúšky v študijnom programe Aplikovaná biológia na FPV UCM v Trnave (bakalárske, magisterské, rigorózne štúdium)
  • člen komisie pre štátne skúšky v študijnom programe Molekulárna biológia na FPV UCM v Trnave (doktorandské štúdium)
  • člen vedeckej rady Fakulty prírodných vied UCM Trnava
  • člen komisie pre obhajoby doktorských dizertácií pre molekulárnu biológiu, člen

Účasť na riešení vedecko-výskumných projektov za posledné roky:

  • VEGA (od roku 1996)
  • APVV (LPP 2009)

Organizátorská a editorská činnosť:

  • zakladateľ a hlavný organizátor série medzinárodných konferencií o enzýmoch z alfa-amylázovej rodiny – ALAMY – od roku 2001 https://www.degruyter.com/view/j/amylase konajú každé tri roky (2001, 2004, 2007, 2010, 2013, 2016, 2019) na Slovensku v Kongresovom centre SAV na Smolenickom zámku: https://imb.savba.sk/~janecek/Alamys/
  • zakladateľ a hlavný editor časopisu “Amylase”;  časopis “Amylase”: zakladateľ a Editor-in-Chief;
  • časopis “3Biotech”: Associate Editor;
  • časopis “Biologia”, section Cellular and Molecular Biology: Managing Editor.
  • časopis “Enzyme and Microbial Technology”: Editorial Board Member.
  • Ad hoc recenzent pre časopisy v odbore Life Sciences.

Spolupráca v zahraničí:

  • Prof. Birte Svensson, Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Kgs. Lyngby – Copenhagen, Dánsko
  • Prof. Marc J.E.C. van der Maarel, Department Aquatic Biotechnology and Bioproduct Engineering, University of Groningen, Groningen, Holandsko
  • Dr. Dessy Natalia, Biochemistry Research Division, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Bandung, Indonézia
  • Dr. Kian Mau Goh, Department of Biosciences and Health Sciences, Universiti Teknologi Malaysia, Johor Bahru, Malajzia
  • Dr. Jean-Luc Da Lage, Laboratoire Evolution, Génomes Comportement, Ecologie, CNRS, Université Paris Sud, Gif sur Yvette, Francúzko
  • Dr. Natasa Bozic, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Belgrade, Srbsko
  • Dr. Paweł Filipkowski, Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Poľsko
  • Dr. Matthew S. Gentry, Department of Molecular and Cellular Biochemistry, Epilepsy and Brain Metabolism Alliance, and Epilepsy Research Center, University of Kentucky College of Medicine, Lexington, KY, USA

Ocenenia:

  • Cena SAV – 1997 a 2013
  • Cena rektora UCM v Trnave – 2015

Vybrané publikácie:

  1. Janecek, S. (1992). New conserved amino acid region of α-amylases in the third loop of their (β/α) 8-barrel domains. Biochemical Journal288(3), 1069-1070.
  2. Janeček, Š. (1994). Sequence similarities and evolutionary relationships of microbial, plant and animal α‐amylases. European journal of biochemistry224(2), 519-524.
  3. Janecek, S., MacGregor, E. A., & Svensson, B. (1995). Characteristic differences in the primary structure allow discrimination of cyclodextrin glucanotransferases from alpha-amylases. Biochemical Journal305(Pt 2), 685.
  4. Janec̆ek, S. (1997). α-Amylase family: molecular biology and evolution. Progress in biophysics and molecular biology67(1), 67-97.
  5. Janecek, S., Svensson, B., & Henrissat, B. (1997). Domain evolution in the α-amylase family. Journal of molecular evolution45(3), 322-331.
  6. Janeček, Š., Lévêque, E., Belarbi, A., & Haye, B. (1999). Close evolutionary relatedness of α-amylases from archaea and plants. Journal of molecular evolution48(4), 421-426.
  7. Janeček, Š., & Ševčı́k, J. (1999). The evolution of starch-binding domain. FEBS letters456(1), 119-125.
  8. Lévêque, E., Janeček, Š., Haye, B., & Belarbi, A. (2000). Thermophilic archaeal amylolytic enzymes. Enzyme and microbial technology26(1), 3-14.
  9. MacGregor, E. A., Janeček, Š., & Svensson, B. (2001). Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology1546(1), 1-20.
  10. Oslancova, A., & Janeček, Š. (2002). Oligo-1, 6-glucosidase and neopullulanase enzyme subfamilies from the α-amylase family defined by the fifth conserved sequence region. Cellular and Molecular Life Sciences CMLS59(11), 1945-1959.
  11. Janeček, Š. (2002). How many conserved sequence regions are there in the α-amylase family. Biologia57(Suppl 11), 29-41.
  12. Janeček, Š., Svensson, B., & MacGregor, E. A. (2003). Relation between domain evolution, specificity, and taxonomy of the α‐amylase family members containing a C‐terminal starch‐binding domain. European Journal of Biochemistry270(4), 635-645.
  13. Da Lage, J. L., Feller, G., & Janeček, Š. (2004). Horizontal gene transfer from Eukarya to Bacteria and domain shuffling: the α-amylase model. Cellular and Molecular Life Sciences CMLS61(1), 97-109.
  14. Zona, R., Chang‐Pi‐Hin, F., O’Donohue, M. J., & Janeček, Š. (2004). Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis. European journal of biochemistry271(14), 2863-2872.
  15. Machovič, M., Svensson, B., Ann MacGregor, E., & Janeček, Š. (2005). A new clan of CBM families based on bioinformatics of starch‐binding domains from families CBM20 and CBM21. The FEBS journal272(21), 5497-5513.
  16. Machovič, M., & Janeček, Š. (2006). Starch-binding domains in the post-genome era. Cellular and Molecular Life Sciences CMLS63(23), 2710-2724.
  17. Machovič, M., & Janeček, Š. (2006). The evolution of putative starch-binding domains. FEBS letters580(27), 6349-6356.
  18. Van der Kaaij, R. M., Janeček, Š., van der Maarel, M. J. E. C., & Dijkhuizen, L. (2007). Phylogenetic and biochemical characterization of a novel cluster of intracellular fungal α-amylase enzymes. Microbiology153(12), 4003-4015.
  19. Godány, A., Vidová, B., & Janeček, Š. (2008). The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved. FEMS microbiology letters284(1), 84-91.
  20. Christiansen, C., Abou Hachem, M., Janeček, Š., Viksø‐Nielsen, A., Blennow, A., & Svensson, B. (2009). The carbohydrate‐binding module family 20–diversity, structure, and function. The FEBS journal276(18), 5006-5029.
  21. Gabriško, M., & Janeček, Š. (2009). Looking for the ancestry of the heavy‐chain subunits of heteromeric amino acid transporters rBAT and 4F2hc within the GH13 α‐amylase family. The FEBS journal276(24), 7265-7278.
  22. Janeček, Š., & Blesák, K. (2011). Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues. The protein journal30(6), 429-435.
  23. Janeček, Š., Svensson, B., & MacGregor, E. A. (2011). Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals. Enzyme and microbial technology49(5), 429-440.
  24. Blesák, K., & Janeček, Š. (2012). Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57. Extremophiles16(3), 497-506.
  25. Janeček, Š., & Kuchtová, A. (2012). In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the α-amylase family GH57. FEBS letters586(19), 3360-3366.
  26. Puspasari, F., Radjasa, O. K., Noer, A. S., Nurachman, Z., Syah, Y. M., van der Maarel, M. J. E. C., Janeček, Š. & Natalia, D. (2013). Raw starch–degrading α‐amylase from B acillus aquimaris MKSC 6.2: isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme. Journal of applied microbiology114(1), 108-120.
  27. Majzlova, K., Pukajova, Z., & Janeček, Š. (2013). Tracing the evolution of the α-amylase subfamily GH13_36 covering the amylolytic enzymes intermediate between oligo-1, 6-glucosidases and neopullulanases. Carbohydrate research367, 48-57.
  28. Da Lage, J. L., Binder, M., Hua-Van, A., Janeček, Š., & Casane, D. (2013). Gene make-up: rapid and massive intron gains after horizontal transfer of a bacterial α-amylase gene to Basidiomycetes. BMC evolutionary biology13(1), 1-13.
  29. Blesak, K., & Janeček, Š. (2013). Two potentially novel amylolytic enzyme specificities in the prokaryotic glycoside hydrolase α-amylase family GH57. Microbiology159(Pt_12), 2584-2593.
  30. Janeček, Š., Svensson, B., & MacGregor, E. A. (2014). α-Amylase: an enzyme specificity found in various families of glycoside hydrolases. Cellular and molecular life sciences71(7), 1149-1170.
  31. Ranjani, V., Janeček, Š., Chai, K. P., Shahir, S., Rahman, R. N. Z. R. A., Chan, K. G., & Goh, K. M. (2014). Protein engineering of selected residues from conserved sequence regions of a novel Anoxybacillus α-amylase. Scientific reports4(1), 1-8.
  32. Kuchtova, A., & Janeček, Š. (2015). In silico analysis of family GH77 with focus on amylomaltases from borreliae and disproportionating enzymes DPE2 from plants and bacteria. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics1854(10), 1260-1268.
  33. Janeček, Š., & Gabriško, M. (2016). Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family. Cellular and Molecular Life Sciences73(14), 2707-2725.
  34. Kuchtova, A., & Janeček, Š. (2016). Domain evolution in enzymes of the neopullulanase subfamily. Microbiology162(12), 2099-2115.
  35. Janeček, Š., Majzlová, K., Svensson, B., & MacGregor, E. A. (2017). The starch‐binding domain family CBM41—An in silico analysis of evolutionary relationships. Proteins: Structure, Function, and Bioinformatics85(8), 1480-1492.
  36. Sarian, F. D., Janeček, Š., Pijning, T., Nurachman, Z., Radjasa, O. K., Dijkhuizen, L., … & van der Maarel, M. J. (2017). A new group of glycoside hydrolase family 13 α-amylases with an aberrant catalytic triad. Scientific reports7(1), 1-10.
  37. Kuchtová, A., Gentry, M. S., & Janeček, Š. (2018). The unique evolution of the carbohydrate‐binding module CBM 20 in laforin. FEBS letters592(4), 586-598.
  38. Martinovičová, M., & Janeček, Š. (2018). In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities. 3 Biotech8(7), 1-11.
  39. Zhang, X., Leemhuis, H., Janeček, Š., Martinovičová, M., Pijning, T., & van der Maarel, M. J. (2019). Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity. Applied microbiology and biotechnology103(15), 6141-6151.
  40. Janeček, Š., Mareček, F., MacGregor, E. A., & Svensson, B. (2019). Starch-binding domains as CBM families–history, occurrence, structure, function and evolution. Biotechnology advances37(8), 107451.
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