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    STUDIA CHEMIA - Issue no. 2%20(Tom%20I%20 / 2010  
         
  Article:   ZINC-CONTAINING ACTIVE SITE IN A PARTIALLY MODIFIED 1GKM CRYSTAL STRUCTURE OF HISTIDINE AMMONIA-LYASE: A COMPUTATIONAL INVESTIGATION.

Authors:  AMALIA-LAURA SEFF, SAROLTA PILBÁK, IOAN SILAGHI-DUMITRESCU, LÁSZLÓ POPPE.
 
       
         
  Abstract:  

The histidine ammonia-lyase (HAL) biocatalyst has an important role in the formation of (E)-urocanic acid from L-histidine eliminating ammonia. In order to investigate the active center of HAL, we have prepared “in silico” a HAL model with a compact active center on the basis of the recently appeared phenylalanine ammonia-lyase (PAL) structure (PDB code: 3CZO). Furthermore, to have a better view on the orientation of a key reaction intermediate within the active site, systematic conformational analysis has been performed. Furthermore, the possible positions of the L-histidine/(E)-urocanic acid were evaluated by optimization and docking.

 

Keywords: histidine ammonia-lyase, homology modeling, conformational analysis, docking, Zn2+

 
         
     
         
         
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