Zinc-containing active site in a partially modified 1GKM crystal structure of histidine ammonia-lyase: A computational investigation

Amalia Laura Seff, Sarolta Pilbák, Ioan Silaghi-Dumitrescu, László Poppe

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)37-45
Number of pages9
JournalStudia Universitatis Babes-Bolyai Chemia
Volume2
Issue number1
Publication statusPublished - Oct 8 2010

Keywords

  • Conformational analysis
  • Docking
  • Histidine ammonia-lyase
  • Homology modeling
  • Zn

ASJC Scopus subject areas

  • Chemistry(all)

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