Full CV
| Attachment | Size |
|---|---|
 CV_Bouriotis.pdf | 81.53 KB |
| Papers_Bouriotis.pdf | 81.88 KB |
Scientific interests
Enzyme Biotechnology
Polysaccharide deacetylases (peptidoglycan deacetylases, chitin deacetylases)
Cold adapted enzymes
See also IMBB home page.
Recent publications
- “Peptidoglycan N- Acetylglucosamine Deacetylases from Bacillus cereus, Highly Conserved Proteins in Bacillus anthracis” E. PSYLINAKIS, I.G. BONECA, K. MAVROMATIS, A. DELI, E. HAYHURST, S. J. FOSTER, K. M. VARUM and V. BOURIOTIS (2005): J.Biol.Chemistry(280),(35) , 30856-30863
- “Crystal Structure of Alkaline Phosphatase from the Antarctic Bacterium TAB5” E. WANG, D. KOUTSIOULIS, H.-K. S. LEIROS, O. A. ANDERSEN, V. BOURIOTIS, E. HOUGH and P. HEIKINHEIMO (2007), J. Mol. Biol. 366, 1318-1331
- “Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase” D. KOUTSIOULIS, E. WANG, M. TZANODASKALAKI, D. NIKIFORAKI, A. DELI, G. FELLER, P. HEIKINHEIMO, and V. BOURIOTIS (2008), Protein Engineering, Design&Selection : vol.21 no.5 pp. 319-327
- “Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatases” D. KOUTSIOULIS, A. LYSKOWSKI, S. MAKI, E. GUTHRIE, G. FELLER, V. BOURIOTIS and P. HEIKINHEIMO, (2010), Protein Science: 19(1):75-84
- “LmbE proteins from Bacillus cereus are de-N-acetylases with broad substrate specificity and are highly similar to proteins in Bacillus anthracis” A. DELI, D. KOUTSIOULIS, V.FADOULOGLOU, P. SPILIOTOPOULOU, BALOMENOU S, ARNAOUTELI S, TZANODASKALAKI M, K. MAVROMATIS, M. KOKKINIDIS and V. BOURIOTIS (2010), FEBS Journal, 277 (13): 2740-2753.