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  1. 1.   Generalized enzymatic mechanism of catalysis by tetrameric L-asparaginases from mesophilic bacteria
  2. Strzelczyk,Pawel; Zhang,Di; Dyba,Marzena; Wlodawer,Alexander; Lubkowski,Jacek
  3. SCIENTIFIC REPORTS. 2020, OCT 15; 10(1):
  1. 2.   Atomic resolution structure of Erwinia chrysanthemi L- asparaginase
  2. Lubkowski, J.; Dauter, M.; Aghaiypour, K.; Wlodawer, A.; Dauter, Z.
  3. Acta Crystallographica Section D-Biological Crystallography. 2003 59(Part 1): 84-92.
  1. 3.   Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups
  2. Jaskolski, M.; Kozak, M.; Lubkowski, J.; Palm, G.; Wlodawer, A.
  3. Acta Crystallographica Section D-Biological Crystallography. 2001 57(Pt. 3): 369-377.
  1. 4.   Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr- Glu?
  2. Aghaiypour, K.; Wlodawer, A.; Lubkowski, J.
  3. Biochimica Et Biophysica Acta-Protein Structure and Molecular Enzymology. 2001 1550(2): 117-128.
  1. 5.   Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase
  2. Aghaiypour, K.; Wlodawer, A.; Lubkowski, J.
  3. Biochemistry. 2001 40(19): 5655-5664.
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