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  1. 1.   Clarification of the Mechanism of Acylation Reaction and Origin of Substrate Specificity of the Serine-Carboxyl Peptidase Sedolisin through QM/MM Free Energy Simulations
  2. Xu, Q.; Yao, J. Z.; Wlodawer, A.; Guo, H.
  3. Journal of Physical Chemistry B. 2011, Mar; 115(10): 2470-2476.
  1. 2.   The QM/MM molecular dynamics and free energy simulations of the acylation reaction catalyzed by the serine-carboxyl peptidase kumamolisin-As
  2. Xu, Q.; Guo, H. B.; Wlodawer, A.; Nakayama, T.; Guo, H.
  3. Biochemistry. 2007, Mar; 46(12): 3784-3792.
  1. 3.   A general acid-base mechanism for the stabilization of a tetrahedral adduct in a serine-carboxyl peptidase: A computational study
  2. Guo, H. B.; Wlodawer, A.; Guo, H.
  3. Journal of the American Chemical Society. 2005, NOV 16; 127(45): 15662-15663.
  1. 4.   Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate
  2. Wlodawer, A.; Li, M.; Gustchina, A.; Oyama, H.; Oda, K.; Beyer, B. B.; Clemente, J.; Dunn, B. M.
  3. Biochemical and Biophysical Research Communications. 2004 314(2): 638-645.
  1. 5.   Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases
  2. Wlodawer, A.; Li, M.; Gustchina, A.; Oyama, H.; Dunn, B. M.; Oda, K.
  3. Acta Biochimica Polonica. 2003 50(1): 81-102.
  1. 6.   Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
  2. Wlodawer, A.; Li, M.; Dauter, Z.; Gustchina, A.; Uchida, K.; Oyama, H.; Dunn, B. M.; Oda, K.
  3. Nature Structural Biology. 2001 8(5): 442-446.
  1. 7.   Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 angstrom
  2. Devedjiev, Y.; Dauter, Z.; Kuznetsov, S. R.; Jones, T. L. Z.; Derewenda, Z. S.
  3. Structure. 2000 8(11): 1137-1146.
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